Updated on 2024/10/15

Information

 

写真a

 
YANAKA SAEKO
 
Organization
Faculty of Pharmaceutical Sciences Department of Pharmaceutical Health Care and Sciences Associate Professor
Title
Associate Professor
Contact information
メールアドレス
Tel
0926426554
Profile
グローバルヘルスケア分野での活動を通じた研究・教育

Research Areas

  • Life Science / Pharmaceutical analytical chemistry and physicochemistry

  • Life Science / Biophysics

Degree

  • Ph. D. (Life Science)

Research History

  • Tokyo Institute of Technology Institute of Innovative Research Associate Professor

    2024.4 - Present

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  • 九州大学大学院 薬学研究院 講師

    2022.9 - 2024.3

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  • National Institutes of Natural Sciences Assistant Professor

    2017.11 - 2022.8

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  • 2011年4月〜2013年3月 日本学術振興会特別研究員(DC2) 東京大学大学院新領域創成科学研究科に所属 2013年4月〜2015年6月日本学術振興会特別研究員(PD) (公財)サントリー生命科学財団、京都大学工学研究科に所属 2015年7月〜2017年10月 自然科学研究機構 分子科学研究所 特任助教 2017年11月〜 自然科学研究機構 分子科学研究所 助教

Research Interests・Research Keywords

  • Research theme:Biomolecular engineering

    Keyword:Biomolecular engineering

    Research period: 2024

  • Research theme:Nuclear Magnetic Resonance

    Keyword:Nuclear Magnetic Resonance

    Research period: 2024

  • Research theme:Elucidation of the molecular mechanism of antibodies expressing their functions through dynamic molecular assembly by structural biological approach

    Keyword:antibody, molecular assembly, structural biology

    Research period: 2015.7 - 2026.9

Awards

  • 物理系薬学部会奨励賞

    2021.3   日本薬学会 物理系薬学部会   抗体の3次元構造と相互作用のダイナミクスを解明する方法の開発と抗体の高機能化への展開

  • 第32回井上研究奨励賞

    2015.2   井上科学振興財団  

  • 若手ポスター賞Ⅰ

    2013.11   日本核磁気共鳴学会  

  • 若手奨励賞

    2013.6   日本蛋白質科学会  

  • 第四回"Merck Award for Young Biochemistry Researcher"優秀賞

    2011.9   メルク株式会社  

  • 修士論文発表会・優秀研究論文賞

    2010.3   東京大学大学院新領域創成科学研究科メディカルゲノム専攻  

  • 英語論文発表会・最優秀賞

    2008.12   東京大学大学院新領域創成科学研究科メディカルゲノム専攻  

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Papers

  • Key role of Pro230 in the hinge region on the IgG architecture and function

    Yuuki Koseki, Yuki Yamaguchi, Michihiko Aoyama, Minoru Tada, Akinobu Senoo, Akiko Ishii-Watabe, Takayuki Uchihashi, Susumu Uchiyama, Koichi Kato, Saeko Yanaka, Jose M.M. Caaveiro

    2024.5

  • Negative interference with antibody-dependent cellular cytotoxicity mediated by rituximab from its interactions with human serum proteins Reviewed

    Saeko Yanaka, Rina Yogo, Hirokazu Yagi, Masayoshi Onitsuka, Natsumi Wakaizumi, Yuki Yamaguchi, Susumu Uchiyama, Koichi Kato

    Frontiers in Immunology   14   1090898   2023.1   ISSN:1664-3224 eISSN:1664-3224

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    <jats:p>Although interactions of small molecular drugs with serum proteins have been widely studied from pharmacokinetic and pharmacodynamic perspectives, there have been few reports on the effects of serum components on therapeutic antibody functions. This study reports the effect of abundant serum proteins on antibody-dependent cellular cytotoxicity (ADCC) mediated by rituximab and Fcγ receptor III (FcγRIII). Human serum albumin (HSA) and the Fab fragment from the pooled serum polyclonal IgG were found to compromise ADCC as non-competitive inhibitors. Our nuclear magnetic resonance data provided direct evidence for the interactions of HSA with both the Fab and Fc regions of rituximab and also with the extracellular region of FcγRIII (sFcγRIII). The degree of involvement in the interaction decreased in the order of rituximab-Fab &amp;gt; rituximab-Fc &amp;gt; sFcγRIII, suggesting preferential binding of HSA to net positively charged proteins. Although much less pronounced than the effect of HSA, polyclonal IgG-Fab specifically interacted with rituximab-Fc. The NMR data also showed that the serum protein interactions cover the Fc surface extensively, suggesting that they can act as pan-inhibitors against various Fc receptor-mediated functions and pharmacokinetics. Our findings highlight the importance of considering serum–protein interactions in the design and application of antibody-based drugs with increased efficacy and safety.</jats:p>

    DOI: 10.3389/fimmu.2023.1090898

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  • Quantitative Visualization of the Interaction between Complement Component C1 and Immunoglobulin G: The Effect of CH1 Domain Deletion Reviewed

    Saeko Yanaka, Shigetaka Nishiguchi, Rina Yogo, Hiroki Watanabe, Jiana Shen, Hirokazu Yagi, Takayuki Uchihashi, Koichi Kato

    International Journal of Molecular Sciences   23 ( 4 )   2090 - 2090   2022.2   ISSN:16616596 eISSN:1422-0067

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    Immunoglobulin G (IgG) adopts a modular multidomain structure that mediates antigen recognition and effector functions, such as complement-dependent cytotoxicity. IgG molecules are self-assembled into a hexameric ring on antigen-containing membranes, recruiting the complement component C1q. In order to provide deeper insights into the initial step of the complement pathway, we report a high-speed atomic force microscopy study for the quantitative visualization of the interaction between mouse IgG and the C1 complex composed of C1q, C1r, and C1s. The results showed that the C1q in the C1 complex is restricted regarding internal motion, and that it has a stronger binding affinity for on-membrane IgG2b assemblages than C1q alone, presumably because of the lower conformational entropy loss upon binding. Furthermore, we visualized a 1:1 stoichiometric interaction between C1/C1q and an IgG2a variant that lacks the entire CH1 domain in the absence of an antigen. In addition to the canonical C1q-binding site on Fc, their interactions are mediated through a secondary site on the CL domain that is cryptic in the presence of the CH1 domain. Our findings offer clues for novel-modality therapeutic antibodies.

    DOI: 10.3390/ijms23042090

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  • Glutamine-free mammalian expression of recombinant glycoproteins with uniform isotope labeling: an application for NMR analysis of pharmaceutically relevant Fc glycoforms of human immunoglobulin G1 Reviewed International journal

    Saeko Yanaka, Hirokazu Yagi, Rina Yogo, Masayoshi Onitsuka, Koichi Kato

    Journal of Biomolecular NMR   76 ( 1-2 )   17 - 22   2022.1   ISSN:09252738

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    Mammalian cells are widely used for producing recombinant glycoproteins of pharmaceutical interest. However, a major drawback of using mammalian cells is the high production costs associated with uniformly isotope-labeled glycoproteins due to the large quantity of labeled L-glutamine required for their growth. To address this problem, we developed a cost-saving method for uniform isotope labeling by cultivating the mammalian cells under glutamine-free conditions, which was achieved by co-expression of glutamine synthase. We demonstrate the utility of this approach using fucosylated and non-fucosylated Fc glycoforms of human immunoglobulin G1.

    DOI: 10.1007/s10858-021-00387-5

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  • NMR assignments of the N-glycans of the Fc fragment of mouse immunoglobulin G2b glycoprotein. International journal

    Saeko Yanaka, Yoshiki Yamaguchi, Takeshi Takizawa, Yohei Miyanoiri, Rina Yogo, Ichio Shimada, Koichi Kato

    Biomolecular NMR assignments   15 ( 1 )   187 - 192   2021.1

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    DOI: 10.1007/s12104-020-10004-5

  • Biophysical characterization of dynamic structures of immunoglobulin G. Reviewed International journal

    Saeko Yanaka, Rina Yogo, Koichi Kato

    Biophysical reviews   2020.5

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    DOI: 10.1007/s12551-020-00698-1

  • On-Membrane Dynamic Interplay between Anti-GM1 IgG Antibodies and Complement Component C1q Reviewed

    Saeko Yanaka, Rina Yogo, Hiroki Watanabe, Yuki Taniguchi, Tadashi Satoh, Naoko Komura, Hiromune Ando, Hirokazu Yagi, Nobuhiro Yuki, Takayuki Uchihashi, Koichi Kato

    International Journal of Molecular Sciences   21 ( 1 )   147 - 147   2019.12

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    DOI: 10.3390/ijms21010147

  • The Fab portion of immunoglobulin G contributes to its binding to Fcγ receptor III Reviewed

    9 ( 1 )   11957   2019.12

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    DOI: 10.1038/s41598-019-48323-w

  • Dynamic Views of the Fc Region of Immunoglobulin G Provided by Experimental and Computational Observations Reviewed

    Saeko Yanaka, Rina Yogo, Rintaro Inoue, Masaaki Sugiyama, Satoru G. Itoh, Hisashi Okumura, Yohei Miyanoiri, Hirokazu Yagi, Tadashi Satoh, Takumi Yamaguchi, Koichi Kato

    Antibodies   8 ( 3 )   2019.7

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    DOI: 10.3390/antib8030039

  • Stable isotope labeling approaches for NMR characterization of glycoproteins using eukaryotic expression systems. Reviewed

    Yanaka S, Yagi H, Yogo R, Yagi-Utsumi M, Kato K

    Journal of biomolecular NMR   71 ( 3 )   193 - 202   2018.2

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    DOI: 10.1007/s10858-018-0169-2

  • NMR Detection of Semi-Specific Antibody Interactions in Serum Environments. Reviewed

    Yanaka S, Yamazaki T, Yogo R, Noda M, Uchiyama S, Yagi H, Kato K

    Molecules (Basel, Switzerland)   22 ( 10 )   2017.9

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    DOI: 10.3390/molecules22101619

  • N-linked protein glycosylation in Nanobdellati (formerly DPANN) archaea and their hosts. Reviewed International journal

    Satoshi Nakagawa, Hiroyuki D Sakai, Shigeru Shimamura, Yoshiki Takamatsu, Shingo Kato, Hirokazu Yagi, Saeko Yanaka, Maho Yagi-Utsumi, Norio Kurosawa, Moriya Ohkuma, Koichi Kato, Ken Takai

    Journal of bacteriology   206 ( 9 )   e0020524   2024.8

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    Members of the kingdom Nanobdellati, previously known as DPANN archaea, are characterized by ultrasmall cell sizes and reduced genomes. They primarily thrive through ectosymbiotic interactions with specific hosts in diverse environments. Recent successful cultivations have emphasized the importance of adhesion to host cells for understanding the ecophysiology of Nanobdellati. Cell adhesion is often mediated by cell surface carbohydrates, and in archaea, this may be facilitated by the glycosylated S-layer protein that typically coats their cell surface. In this study, we conducted glycoproteomic analyses on two co-cultures of Nanobdellati with their host archaea, as well as on pure cultures of both host and non-host archaea. Nanobdellati exhibited various glycoproteins, including archaellins and hypothetical proteins, with glycans that were structurally distinct from those of their hosts. This indicated that Nanobdellati autonomously synthesize their glycans for protein modifications probably using host-derived substrates, despite the high energy cost. Glycan modifications on Nanobdellati proteins consistently occurred on asparagine residues within the N-X-S/T sequon, consistent with patterns observed across archaea, bacteria, and eukaryotes. In both host and non-host archaea, S-layer proteins were commonly modified with hexose, N-acetylhexosamine, and sulfonated deoxyhexose. However, the N-glycan structures of host archaea, characterized by distinct sugars such as deoxyhexose, nonulosonate sugar, and pentose at the nonreducing ends, were implicated in enabling Nanobdellati to differentiate between host and non-host cells. Interestingly, the specific sugar, xylose, was eliminated from the N-glycan in a host archaeon when co-cultured with Nanobdella. These findings enhance our understanding of the role of protein glycosylation in archaeal interactions.IMPORTANCENanobdellati archaea, formerly known as DPANN, are phylogenetically diverse, widely distributed, and obligately ectosymbiotic. The molecular mechanisms by which Nanobdellati recognize and adhere to their specific hosts remain largely unexplored. Protein glycosylation, a fundamental biological mechanism observed across all domains of life, is often crucial for various cell-cell interactions. This study provides the first insights into the glycoproteome of Nanobdellati and their host and non-host archaea. We discovered that Nanobdellati autonomously synthesize glycans for protein modifications, probably utilizing substrates derived from their hosts. Additionally, we identified distinctive glycosylation patterns that suggest mechanisms through which Nanobdellati differentiate between host and non-host cells. This research significantly advances our understanding of the molecular basis of microbial interactions in extreme environments.

    DOI: 10.1128/jb.00205-24

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  • Characterization of high affinity IgM and IgG monoclonal antibodies against norovirus variants GII.4 and GII.17

    Jumpei Tagawa, Saeko Yanaka, Yuri Kato, Akitsu Masuda, Jae Man Lee, Akinobu Senoo, Kosuke Oyama, Motohiro Nishida, Takahiro Kusakabe, Jose M.M. Caaveiro

    2024.5

  • Identification of potential C1-binding sites in the immunoglobulin CL domains Reviewed

    Saeko Yanaka, Atsuji Kodama, Shigetaka Nishiguchi, Rina Hiramine, Jiana Shen, Pornthip Boonsri, Duckyong Sung, Yukiko Isono, Hirokazu Yagi, Yohei Miyanoiri, Takayuki Uchihashi, Koichi Kato

    International Immunology   36 ( 8 )   405 - 412   2024.4   ISSN:0953-8178 eISSN:1460-2377

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    Abstract

    IgG molecules that bind antigen on the membrane of target cells spontaneously form hexameric rings, thus recruiting C1 to initiate the complement pathway. However, our previous report indicated that a mouse IgG mutant lacking the Cγ1 domain activates the pathway independently of antigen presence through its monomeric interaction with C1q via the CL domain, as well as Fc. In this study, we investigated the potential interaction between C1q and human CL isoforms. Quantitative single molecule observations using high-speed atomic force microscopy revealed that human Cκ exhibited comparable C1q binding capabilities with its mouse counterpart, surpassing the Cλ types, which have a higher isoelectric point than the Cκ domains. Nuclear magnetic resonance and mutation experiments indicated that the human and mouse Cκ domains share a common primary binding site for C1q, centered on Glu194, a residue conserved in the Cκ domains but absent in the Cλ domains. Additionally, the Cγ1 domain, with its high isoelectric point, can cause electrostatic repulsion to the C1q head and impede the C1q-interaction adjustability of the Cκ domain in Fab. The removal of the Cγ1 domain is considered to eliminate these factors and thus promote Cκ interaction with C1q with the potential risk of uncontrolled activation of the complement pathway in vivo in the absence of antigen. However, this research underscores the presence of potential subsites in Fab for C1q binding, offering promising targets for antibody engineering to refine therapeutic antibody design.

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  • Quantitative Analysis of Therapeutic Antibody Interactions with Fcγ Receptors Using High-Speed Atomic Force Microscopy Reviewed

    Saeko Yanaka, Hiroki Watanabe, Rina Yogo, Mesayamas Kongsema, Sachiko Kondo, Hirokazu Yagi, Takayuki Uchihashi, Koichi Kato

    Biological & pharmaceutical bulletin   47 ( 1 )   334 - 338   2024.1   ISSN:09186158 eISSN:13475215

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    <p>This study employed high-speed atomic force microscopy to quantitatively analyze the interactions between therapeutic antibodies and Fcγ receptors (FcγRs). Antibodies are essential components of the immune system and are integral to biopharmaceuticals. The focus of this study was on immunoglobulin G molecules, which are crucial for antigen binding <i>via</i> the Fab segments and cytotoxic functions through their Fc portions. We conducted real-time, label-free observations of the interactions of rituximab and mogamulizumab with the recombinant FcγRIIIa and FcγRIIa. The dwell times of FcγR binding were measured at the single-molecule level, which revealed an extended interaction duration of mogamulizumab with FcγRIIIa compared with that of rituximab. This is linked to enhanced antibody-dependent cellular cytotoxicity that is attributed to the absence of the core fucosylation of Fc-linked <i>N</i>-glycan. This study also emphasizes the crucial role of the Fab segments in the interaction with FcγRIIa as well as that with FcγRIIIa. This approach provided quantitative insight into therapeutic antibody interactions and exemplified kinetic proofreading, where cellular discrimination relies on ligand residence times. Observing the dwell times of antibodies on the effector molecules has emerged as a robust indicator of therapeutic antibody efficacy. Ultimately, these findings pave the way for the development of refined therapeutic antibodies with tailored interactions with specific FcγRs. This research contributes to the advancement of biopharmaceutical antibody design and optimizing antibody-based treatments for enhanced efficacy and precision.</p>

    DOI: 10.1248/bpb.b23-00751

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  • Quantitative Analysis of Therapeutic Antibody Interactions with Fcγ Receptors Using High-Speed Atomic Force Microscopy(タイトル和訳中)

    Yanaka Saeko, Watanabe Hiroki, Yogo Rina, Kongsema Mesayamas, Kondo Sachiko, Yagi Hirokazu, Uchihashi Takayuki, Kato Koichi

    Biological & Pharmaceutical Bulletin   47 ( 1 )   334 - 338   2024.1   ISSN:0918-6158

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  • Quantitative Analysis of Therapeutic Antibody Interactions with Fcγ Receptors Using High-Speed Atomic Force Microscopy

    Yanaka, S; Watanabe, H; Yogo, R; Kongsema, M; Kondo, S; Yagi, H; Uchihashi, T; Kato, K

    BIOLOGICAL & PHARMACEUTICAL BULLETIN   47 ( 1 )   334 - 338   2024.1   ISSN:0918-6158 eISSN:1347-5215

  • Characterization of protein glycosylation in an Asgard archaeon. Reviewed International journal

    Satoshi Nakagawa, Hiroyuki Imachi, Shigeru Shimamura, Saeko Yanaka, Hirokazu Yagi, Maho Yagi-Utsumi, Hiroyuki Sakai, Shingo Kato, Moriya Ohkuma, Koichi Kato, Ken Takai

    BBA advances   6   100118 - 100118   2024

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    Archaeal cells are typically enveloped by glycosylated S-layer proteins. Archaeal protein glycosylation provides valuable insights not only into their adaptation to their niches but also into their evolutionary trajectory. Notably, thermophilic Thermoproteota modify proteins with N-glycans that include two GlcNAc units at the reducing end, resembling the "core structure" preserved across eukaryotes. Recently, Asgard archaea, now classified as members of the phylum Promethearchaeota, have offered unprecedented opportunities for understanding the role of archaea in eukaryogenesis. Despite the presence of genes indicative of protein N-glycosylation in this archaeal group, these have not been experimentally investigated. Here we performed a glycoproteome analysis of the firstly isolated Asgard archaeon Promethearchaeum syntrophicum. Over 700 different proteins were identified through high-resolution LC-MS/MS analysis, however, there was no evidence of either the presence or glycosylation of putative S-layer proteins. Instead, N-glycosylation in this archaeon was primarily observed in an extracellular solute-binding protein, possibly related to chemoreception or transmembrane transport of oligopeptides. The glycan modification occurred on an asparagine residue located within the conserved N-X-S/T sequon, consistent with the pattern found in other archaea, bacteria, and eukaryotes. Unexpectedly, three structurally different N-glycans lacking the conventional core structure were identified in this archaeon, presenting unique compositions that included atypical sugars. Notably, one of these sugars was likely HexNAc modified with a threonine residue, similar to modifications previously observed in mesophilic methanogens within the Methanobacteriati. Our findings advance our understanding of Asgard archaea physiology and evolutionary dynamics.

    DOI: 10.1016/j.bbadva.2024.100118

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  • 抗体医薬の作動メカニズムの分子基盤

    谷中 冴子, 加藤 晃一

    生物工学会誌   101 ( 7 )   347 - 349   2023.7   ISSN:09193758 eISSN:24358630

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    Language:Japanese   Publisher:公益社団法人 日本生物工学会  

    DOI: 10.34565/seibutsukogaku.101.7_347

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  • Mutational and Environmental Effects on the Dynamic Conformational Distributions of Lys48-Linked Ubiquitin Chains Reviewed

    Methanee Hiranyakorn, Maho Yagi-Utsumi, Saeko Yanaka, Naoya Ohtsuka, Norie Momiyama, Tadashi Satoh, Koichi Kato

    International Journal of Molecular Sciences   24 ( 7 )   6075   2023.3   ISSN:16616596

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    DOI: 10.3390/ijms24076075

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  • The B Domain of Protein A Retains Residual Structures in 6 M Guanidinium Chloride as Revealed by Hydrogen/Deuterium-Exchange NMR Spectroscopy. Reviewed International journal

    Saeko Yanaka, Maho Yagi-Utsumi, Koichi Kato, Kunihiro Kuwajima

    Protein science : a publication of the Protein Society   32 ( 3 )   e4569   2023.1   ISSN:0961-8368 eISSN:1469-896X

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    The characterization of residual structures persistent in unfolded proteins is an important issue in studies of protein folding, because the residual structures present, if any, may form a folding initiation site and guide the subsequent folding reactions. Here, we studied the residual structures of the isolated B domain (BDPA) of staphylococcal protein A in 6 M guanidinium chloride. BDPA is a small three-helix-bundle protein, and until recently its folding/unfolding reaction has been treated as a simple two-state process between the native and the fully unfolded states. We employed a dimethylsulfoxide (DMSO)-quenched hydrogen/deuterium (H/D)-exchange 2D NMR techniques with the use of spin desalting columns, which allowed us to investigate the H/D-exchange behavior of individually identified peptide amide (NH) protons. We obtained H/D-exchange protection factors of the 21 NH protons that form an α-helical hydrogen bond in the native structure, and the majority of these NH protons were significantly protected with a protection factor of 2.0-5.2 in 6 M guanidinium chloride, strongly suggesting that these weakly protected NH protons form much stronger hydrogen bonds under native folding conditions. The results can be used to deduce the structure of an early folding intermediate, when such an intermediate is shown by other methods. Among three native helical regions, the third helix in the C-terminal side was highly protected and stabilized by side-chain salt bridges, probably acting as the folding initiation site of BDPA. The present results are discussed in relation to previous experimental and computational findings on the folding mechanisms of BDPA. This article is protected by copyright. All rights reserved.

    DOI: 10.1002/pro.4569

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  • The Fab portion of immunoglobulin G has sites in the CL domain that interact with Fc gamma receptor IIIa Reviewed

    Yuki Yamaguchi, Natsumi Wakaizumi, Mine Irisa, Takahiro Maruno, Mari Shimada, Koya Shintani, Haruka Nishiumi, Rina Yogo, Saeko Yanaka, Daisuke Higo, Tetsuo Torisu, Koichi Kato, Susumu Uchiyama

    mAbs   14 ( 1 )   2022.12   ISSN:1942-0862 eISSN:1942-0870

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    DOI: 10.1080/19420862.2022.2038531

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  • Four-dimensional Structures and Molecular Designs of Glycans Reviewed

    Saeko Yanaka

    Trends in Glycoscience and Glycotechnology   34 ( 201 )   E85 - E90   2022.9   ISSN:0915-7352 eISSN:1883-2113

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    DOI: 10.4052/tigg.2042.1e

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  • DMSO-Quenched H/D-Exchange 2D NMR Spectroscopy and Its Applications in Protein Science. Reviewed International journal

    Kunihiro Kuwajima, Maho Yagi-Utsumi, Saeko Yanaka, Koichi Kato

    Molecules (Basel, Switzerland)   27 ( 12 )   2022.6

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    Hydrogen/deuterium (H/D) exchange combined with two-dimensional (2D) NMR spectroscopy has been widely used for studying the structure, stability, and dynamics of proteins. When we apply the H/D-exchange method to investigate non-native states of proteins such as equilibrium and kinetic folding intermediates, H/D-exchange quenching techniques are indispensable, because the exchange reaction is usually too fast to follow by 2D NMR. In this article, we will describe the dimethylsulfoxide (DMSO)-quenched H/D-exchange method and its applications in protein science. In this method, the H/D-exchange buffer is replaced by an aprotic DMSO solution, which quenches the exchange reaction. We have improved the DMSO-quenched method by using spin desalting columns, which are used for medium exchange from the H/D-exchange buffer to the DMSO solution. This improvement has allowed us to monitor the H/D exchange of proteins at a high concentration of salts or denaturants. We describe methodological details of the improved DMSO-quenched method and present a case study using the improved method on the H/D-exchange behavior of unfolded human ubiquitin in 6 M guanidinium chloride.

    DOI: 10.3390/molecules27123748

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  • Fungal β‐Mannosyloxymannitol Glycolipids and Their Analogues: Synthesis and Mincle‐Mediated Signaling Activity Reviewed

    Takanori Matsumaru, Kasumi Sakuratani, Saeko Yanaka, Koichi Kato, Sho Yamasaki, Yukari Fujimoto

    European Journal of Organic Chemistry   2022 ( 20 )   2022.5   ISSN:1434-193X eISSN:1099-0690

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    DOI: 10.1002/ejoc.202200109

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    Other Link: https://onlinelibrary.wiley.com/doi/full-xml/10.1002/ejoc.202200109

  • Efficient Visible/NIR Light-driven Uncaging of Hydroxylated Thiazole Orange-based Caged Compounds in Aqueous Media Reviewed

    Ryu Hashimoto, Masafumi Minoshima, Souhei Sakata, Fumihito Ono, Hirokazu Ishii, Yuki Watakabe, Tomomi Nemoto, Saeko Yanaka, Koichi Kato, Kazuya Kikuchi

    Chemical Science   13 ( 25 )   7462 - 7467   2022.2   ISSN:2041-6520 eISSN:2041-6539

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    Language:English   Publishing type:Research paper (scientific journal)   Publisher:Royal Society of Chemistry ({RSC})  

    <jats:p>In the photoactivation strategies with bioactive molecules, one-photon visible or two-photon near-infrared light-sensitive caged compounds are desirable tools for biological applications because they offer reduced phototoxicity and deep tissue penetration....</jats:p>

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  • Biophysical Characterization of Novel DNA Aptamers against K103N/Y181C Double Mutant HIV-1 Reverse Transcriptase. Reviewed International journal

    Siriluk Ratanabunyong, Supaphorn Seetaha, Supa Hannongbua, Saeko Yanaka, Maho Yagi-Utsumi, Koichi Kato, Atchara Paemanee, Kiattawee Choowongkomon

    Molecules (Basel, Switzerland)   27 ( 1 )   2022.1

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    The human immunodeficiency virus type-1 Reverse Transcriptase (HIV-1 RT) plays a pivotal role in essential viral replication and is the main target for antiviral therapy. The anti-HIV-1 RT drugs address resistance-associated mutations. This research focused on isolating the potential specific DNA aptamers against K103N/Y181C double mutant HIV-1 RT. Five DNA aptamers showed low IC50 values against both the KY-mutant HIV-1 RT and wildtype (WT) HIV-1 RT. The kinetic binding affinity forms surface plasmon resonance of both KY-mutant and WT HIV-1 RTs in the range of 0.06-2 μM and 0.15-2 μM, respectively. Among these aptamers, the KY44 aptamer was chosen to study the interaction of HIV-1 RTs-DNA aptamer complex by NMR experiments. The NMR results indicate that the aptamer could interact with both WT and KY-mutant HIV-1 RT at the NNRTI drug binding pocket by inducing a chemical shift at methionine residues. Furthermore, KY44 could inhibit pseudo-HIV particle infection in HEK293 cells with nearly 80% inhibition and showed low cytotoxicity on HEK293 cells. These together indicated that the KY44 aptamer could be a potential inhibitor of both WT and KY-mutant HIV-RT.

    DOI: 10.3390/molecules27010285

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  • Desiccation-induced fibrous condensation of CAHS protein from an anhydrobiotic tardigrade. International journal

    Maho Yagi-Utsumi, Kazuhiro Aoki, Hiroki Watanabe, Chihong Song, Seiji Nishimura, Tadashi Satoh, Saeko Yanaka, Christian Ganser, Sae Tanaka, Vincent Schnapka, Ean Wai Goh, Yuji Furutani, Kazuyoshi Murata, Takayuki Uchihashi, Kazuharu Arakawa, Koichi Kato

    Scientific reports   11 ( 1 )   21328 - 21328   2021.11

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    DOI: 10.1038/s41598-021-00724-6

  • Tardigrade Secretory-Abundant Heat-Soluble Protein Has a Flexible β-Barrel Structure in Solution and Keeps This Structure in Dehydration. International journal

    125 ( 32 )   9145 - 9154   2021.8

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    Secretory-abundant heat-soluble (SAHS) proteins are unique heat-soluble proteins of Tardigrada and are believed to play an essential role in anhydrobiosis, a latent state of life induced by desiccation. To investigate the dynamic properties, molecular dynamics (MD) simulations of a SAHS protein, RvSAHS1, were performed in solution and under dehydrating conditions. For comparison purposes, MD simulations of a human liver-type fatty-acid binding protein (LFABP) were performed in solution. Furthermore, high-speed atomic force microscopy observations were conducted to ascertain the results of the MD simulations. Three properties of RvSAHS1 were found as follows. (1) The entrance region of RvSAHS1 is more flexible and can be more extensive in solutions compared with that of a human LFABP because there is no salt bridge between the βD and βE strands. (2) The intrinsically disordered domain in the N-terminal region significantly fluctuates and can form an amphiphilic α-helix. (3) The size of the entrance region gets smaller along with dehydration, keeping the β-barrel structure. Overall, the obtained results provide atomic-level dynamics of SAHS proteins.

    DOI: 10.1021/acs.jpcb.1c04850

  • Structural and Functional Roles of the N-Glycans in Therapeutic Antibodies

    Hirokazu Yagi, Saeko Yanaka, Koichi Kato

    Comprehensive Glycoscience   534 - 542   2021.6

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    DOI: 10.1016/b978-0-12-819475-1.00044-4

  • Investigation of RT1t49 aptamer binding to human immunodeficiency virus 1 reverse transcriptase

    {Supa Hannongbua}

    JOURNAL OF CURRENT SCIENCE AND TECHNOLOGY   11 ( 1 )   2021.4

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    DOI: 10.14456/JCST.2021.8

  • Metal complex lipids for fluid-fluid phase separation in co-assembled phospholipid membranes. International journal

    Ryo Ohtani, Yuka Anegawa, Hikaru Watanabe, Yutaro Tajima, Masanao Kinoshita, Nobuaki Matsumori, Kenichi Kawano, Saeko Yanaka, Koichi Kato, Masaaki Nakamura, Masaaki Ohba, Shinya Hayami

    Angewandte Chemie (International ed. in English)   60 ( 24 )   13603 - 13608   2021.3

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    DOI: 10.1002/anie.202102774

  • Comprehensive characterization of oligosaccharide conformational ensembles with conformer classification by free-energy landscape via reproductive kernel Hilbert space

    Tokio Watanabe, Hirokazu Yagi, Saeko Yanaka, Takumi Yamaguchi, Koichi Kato

    Physical Chemistry Chemical Physics   2021.3

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    DOI: 10.1039/d0cp06448c

  • A feasibility study of inverse contrast-matching small-angle neutron scattering method combined with size exclusion chromatography using antibody interactions as model systems. International journal

    Nobuhiro Sato, Rina Yogo, Saeko Yanaka, Anne Martel, Lionel Porcar, Ken Morishima, Rintaro Inoue, Taiki Tominaga, Takao Arimori, Junichi Takagi, Masaaki Sugiyama, Koichi Kato

    Journal of biochemistry   2021.2

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    DOI: 10.1093/jb/mvab012

  • Characterization of new DNA Aptamers for anti-HIV-1 Reverse Transcriptase. International journal

    Supa Hannongbua, Siriluk Ratanabunyong, Niran Aeksiri, Saeko Yanaka, Maho Yagi-Utsumi, Koichi Kato, Kiattawee Choowongkomol

    Chembiochem : a European journal of chemical biology   22 ( 5 )   915 - 923   2020.10

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    DOI: 10.1002/cbic.202000633

  • Silkworm Pupae Function as Efficient Producers of Recombinant Glycoproteins with Stable-Isotope Labeling. International journal

    Hirokazu Yagi, Saeko Yanaka, Rina Yogo, Akari Ikeda, Masayoshi Onitsuka, Toshio Yamazaki, Tatsuya Kato, Enoch Y Park, Jun Yokoyama, Koichi Kato

    Biomolecules   10 ( 11 )   2020.10

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    DOI: 10.3390/biom10111482

  • Residual Structure of Unfolded Ubiquitin as Revealed by Hydrogen/Deuterium-Exchange 2D NMR. International journal

    Maho Yagi-Utsumi, Mahesh S Chandak, Saeko Yanaka, Methanee Hiranyakorn, Takashi Nakamura, Koichi Kato, Kunihiro Kuwajima

    Biophysical journal   119 ( 10 )   2029 - 2038   2020.10

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    DOI: 10.1016/j.bpj.2020.10.003

  • NMR Characterization of Conformational Interconversions of Lys48-Linked Ubiquitin Chains Reviewed

    Methanee Hiranyakorn, Saeko Yanaka, Tadashi Satoh, Thunchanok Wilasri, Benchawan Jityuti, Maho Yagi-Utsumi, Koichi Kato

    International Journal of Molecular Sciences   21 ( 15 )   5351 - 5351   2020.7

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    DOI: 10.3390/ijms21155351

  • Pseudo-membrane jackets: Two-dimensional coordination polymers achieving visible phase separation in cell membrane. Reviewed International journal

    Ryo Ohtani, Kenichi Kawano, Masanao Kinoshita, Saeko Yanaka, Hikaru Watanabe, Kenji Hirai, Shiroh Futaki, Nobuaki Matsumori, Hiroshi Uji-I, Masaaki Ohba, Koichi Kato, Shinya Hayami

    Angewandte Chemie (International ed. in English)   59 ( 41 )   17931 - 17937   2020.6

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    DOI: 10.1002/anie.202006600

  • Characterization of amyloid β fibril formation under microgravity conditions. Reviewed International journal

    6   17 - 17   2020.6

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    Amyloid fibrils are self-assembled and ordered proteinaceous supramolecules structurally characterized by the cross-β spine. Amyloid formation is known to be related to various diseases typified by neurogenerative disorders and involved in a variety of functional roles. Whereas common mechanisms for amyloid formation have been postulated across diverse systems, the mesoscopic morphology of the fibrils is significantly affected by the type of solution condition in which it grows. Amyloid formation is also thought to share a phenomenological similarity with protein crystallization. Although many studies have demonstrated the effect of gravity on protein crystallization, its effect on amyloid formation has not been reported. In this study, we conducted an experiment at the International Space Station (ISS) to characterize fibril formation of 40-residue amyloid β (Aβ(1-40)) under microgravity conditions. Our comparative analyses revealed that the Aβ(1-40) fibrilization progresses much more slowly on the ISS than on the ground, similarly to protein crystallization. Furthermore, microgravity promoted the formation of distinct morphologies of Aβ(1-40) fibrils. Our findings demonstrate that the ISS provides an ideal experimental environment for detailed investigations of amyloid formation mechanisms by eliminating the conventionally uncontrollable factors derived from gravity.

    DOI: 10.1038/s41526-020-0107-y

  • Current status and issues of protein solution biophysics-Session 1SDP. Reviewed International journal

    Saeko Yanaka, Susumu Uchiyama

    Biophysical reviews   12 ( 2 )   263 - 264   2020.4

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    DOI: 10.1007/s12551-020-00671-y

  • Editorial for the Special Issue of Biophysical Reviews focused on the Biophysical Society of Japan with select scientific content from the 57th BSJ annual meeting, Miyazaki, Japan. Reviewed International journal

    Tamiki Komatsuzaki, Haruki Nakamura, Jeremy Tame, Saeko Yanaka, Takeharu Nagai, Kuniaki Nagayama

    Biophysical reviews   12 ( 2 )   183 - 185   2020.3

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    DOI: 10.1007/s12551-020-00691-8

  • Newly developed Laboratory-based Size exclusion chromatography Small-angle x-ray scattering System (La-SSS) Reviewed

    Rintaro Inoue, Tatsuo Nakagawa, Ken Morishima, Nobuhiro Sato, Aya Okuda, Reiko Urade, Rina Yogo, Saeko Yanaka, Maho Yagi-Utsumi, Koichi Kato, Kazuki Omoto, Kazuki Ito, Masaaki Sugiyama

    Scientific Reports   9 ( 1 )   12610   2019.12

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    DOI: 10.1038/s41598-019-48911-w

  • Structural and thermodynamic basis for the recognition of the substrate-binding cleft on hen egg lysozyme by a single-domain antibody Reviewed

    Hiroki Akiba, Hiroko Tamura, Masato Kiyoshi, Saeko Yanaka, Kenji Sugase, Jose M. M. Caaveiro, Kouhei Tsumoto

    Scientific Reports   9 ( 1 )   15481   2019.12

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    DOI: 10.1038/s41598-019-50722-y

  • Remodeling of the Oligosaccharide Conformational Space in the Prebound State To Improve Lectin-Binding Affinity. Reviewed International journal

    Tatsuya Suzuki, Saeko Yanaka, Tokio Watanabe, Gengwei Yan, Tadashi Satoh, Hirokazu Yagi, Takumi Yamaguchi, Koichi Kato

    Biochemistry   59 ( 34 )   3180 - 3185   2019.10

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    DOI: 10.1021/acs.biochem.9b00594

  • Mutational and Combinatorial Control of Self-Assembling and Disassembling of Human Proteasome α Subunits Reviewed

    20 ( 9 )   2308 - 2308   2019.5

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    DOI: 10.3390/ijms20092308

  • Enabling adoption of 2D-NMR for the higher order structure assessment of monoclonal antibody therapeutics. Reviewed

    mAbs   2018.12

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    DOI: 10.1080/19420862.2018.1544454

  • Backbone 1H, 13C, and 15N assignments of the extracellular region of human Fcγ receptor IIIb. Reviewed International journal

    12 ( 1 )   201 - 204   2018.2

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    DOI: 10.1007/s12104-018-9809-4

  • Structure and Dynamics of Immunoglobulin G Glycoproteins. Reviewed

    Yagi H, Yanaka S, Kato K

    Advances in experimental medicine and biology   1104   219 - 235   2018.1

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    DOI: 10.1007/978-981-13-2158-0_11

  • Theoretical and Experimental Studies on Inclusion Complexes of Pinostrobin and β-Cyclodextrins. Reviewed

    86 ( 1 )   2018.1

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    DOI: 10.3390/scipharm86010005

  • Conformational effects of N-glycan core fucosylation of immunoglobulin G Fc region on its interaction with Fcγ receptor IIIa. Reviewed

    7 ( 1 )   13780   2017.10

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    DOI: 10.1038/s41598-017-13845-8

  • Formation of the chaperonin complex studied by 2D NMR spectroscopy. Reviewed

    Takenaka T, Nakamura T, Yanaka S, Yagi-Utsumi M, Chandak MS, Takahashi K, Paul S, Makabe K, Arai M, Kato K, Kuwajima K

    PloS one   12 ( 10 )   e0187022   2017.10

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    DOI: 10.1371/journal.pone.0187022

  • Characterization of conformational deformation-coupled interaction between immunoglobulin G1 Fc glycoprotein and a low-affinity Fcγ receptor by deuteration-assisted small-angle neutron scattering. Reviewed

    12   1 - 4   2017.8

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    DOI: 10.1016/j.bbrep.2017.08.004

  • Elucidation of potential sites for antibody engineering by fluctuation editing Reviewed

    Saeko Yanaka, Yoshitaka Moriwaki, Kouhei Tsumoto, Kenji Sugase

    SCIENTIFIC REPORTS   7 ( 1 )   9597   2017.8

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    DOI: 10.1038/s41598-017-10246-9

  • Exploration of the Conformational Dynamics of Major Histocompatibility Complex Molecules Reviewed

    Saeko Yanaka, Kenji Sugase

    FRONTIERS IN IMMUNOLOGY   8   632   2017.5

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    DOI: 10.3389/fimmu.2017.00632

  • Hyper-Assembly of Self-Assembled Glycoclusters Mediated by Specific Carbohydrate-Carbohydrate Interactions Reviewed

    Gengwei Yan, Takumi Yamaguchi, Tatsuya Suzuki, Saeko Yanaka, Sota Sato, Makoto Fujita, Koichi Kato

    CHEMISTRY-AN ASIAN JOURNAL   12 ( 9 )   968 - 972   2017.5

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    DOI: 10.1002/asia.201700202

  • Conformational Analysis of a High-Mannose-Type Oligosaccharide Displaying Glucosyl Determinant Recognised by Molecular Chaperones Using NMR-Validated Molecular Dynamics Simulation. Reviewed International journal

    Tatsuya Suzuki, Megumi Kajino, Saeko Yanaka, Tong Zhu, Hirokazu Yagi, Tadashi Satoh, Takumi Yamaguchi, Koichi Kato

    Chembiochem : a European journal of chemical biology   18 ( 4 )   396 - 401   2017.2

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    DOI: 10.1002/cbic.201600595

  • Quantitative analysis of protein-ligand interactions by NMR Reviewed

    Ayako Furukawa, Tsuyoshi Konuma, Saeko Yanaka, Kenji Sugase

    PROGRESS IN NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY   96   47 - 57   2016.8

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    DOI: 10.1016/j.pnmrs.2016.02.002

  • Peptide-dependent Conformational Fluctuation Determines the Stability of the Human Leukocyte Antigen Class I Complex Reviewed

    Saeko Yanaka, Takamasa Ueno, Yi Shi, Jianxun Qi, George F. Gao, Kouhei Tsumoto, Kenji Sugase

    JOURNAL OF BIOLOGICAL CHEMISTRY   289 ( 35 )   24680 - 24690   2014.8

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    DOI: 10.1074/jbc.M114.566174

  • Hyperthin nanochains composed of self-polymerizing protein shackles Reviewed

    Ryo Matsunaga, Saeko Yanaka, Satoru Nagatoishi, Kouhei Tsumoto

    NATURE COMMUNICATIONS   4   2211   2013.7

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    DOI: 10.1038/ncomms3211

  • Interleukin-11 Links Oxidative Stress and Compensatory Proliferation Reviewed

    Takashi Nishina, Sachiko Komazawa-Sakon, Saeko Yanaka, Xuehua Piao, Dong-Mei Zheng, Jiang-Hu Piao, Yuko Kojima, Shunhei Yamashina, Emiko Sano, Tracy Putoczki, Takahiro Doi, Takashi Ueno, Junji Ezaki, Hiroko Ushio, Matthias Ernst, Kouhei Tsumoto, Ko Okumura, Hiroyasu Nakano

    SCIENCE SIGNALING   5 ( 207 )   ra5   2012.1

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    DOI: 10.1126/scisignal.2002056

  • Non-core Region Modulates Interleukin-11 Signaling Activity GENERATION OF AGONIST AND ANTAGONIST VARIANTS Reviewed

    Saeko Yanaka, Emiko Sano, Norio Naruse, Kin-ichiro Miura, Mutsumi Futatsumori-Sugai, Jose M. M. Caaveiro, Kouhei Tsumoto

    JOURNAL OF BIOLOGICAL CHEMISTRY   286 ( 10 )   8085 - 8093   2011.3

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    DOI: 10.1074/jbc.M110.152561

  • Contribution of the flexible loop region to the function of staphylococcal enterotoxin B Reviewed

    Saeko Yanaka, Motonori Kudou, Yoshikazu Tanaka, Takumi Sasaki, Sumiyo Takemoto, Atsuko Sakata, Yukio Hattori, Tomoyuki Koshi, Shiro Futaki, Kouhei Tsumoto, Toshihiro Nakashima

    PROTEIN ENGINEERING DESIGN & SELECTION   23 ( 5 )   415 - 421   2010.5

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    DOI: 10.1093/protein/gzq006

  • Impact of Intrinsic Cooperative Thermodynamics of Peptide-MHC Complexes on Antiviral Activity of HIV-Specific CTL Reviewed

    Chihiro Motozono, Saeko Yanaka, Kouhei Tsumoto, Masafumi Takiguchi, Takamasa Ueno

    JOURNAL OF IMMUNOLOGY   182 ( 9 )   5528 - 5536   2009.5

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    DOI: 10.4049/jimmunol.0803471

  • Isothiocyanate inhibits restitution and wound repair after injury in the stomach: Ex vivo and in vitro studies Reviewed

    Regina Ragasa, Eiji Nakamura, Lisa Marrone, Saeko Yanaka, Shusaku Hayashi, Koji Takeuchi, Susan J. Hagen

    JOURNAL OF PHARMACOLOGY AND EXPERIMENTAL THERAPEUTICS   323 ( 1 )   1 - 9   2007.10

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    DOI: 10.1124/jpet.107.121640

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Presentations

  • Investigation of conformational dynamics and interactions of antibodies towards their functional improvement Invited International conference

    Saeko Yanaka, Koichi Kato

    2023.3 

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    Event date: 2023.3

    Language:Japanese   Presentation type:Oral presentation (general)  

    Country:Japan  

  • Integrative approach for the observation of conformational dynamics and interactions of antibodies Invited International conference

    Saeko Yanaka, Koichi Kato

    The 7th International Symposium on Drug Discovery and Design by NMR  2022.10 

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    Event date: 2022.10

    Language:Japanese   Presentation type:Oral presentation (general)  

    Country:Japan  

  • Multifaceted observation of conformational dynamics and interactions of antibodies Invited International conference

    S. Yanaka, R. Yogo, H. Yagi, K. Kato

    ABA-APPA-TBS Joint Congress in Taiwan  2022.6 

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    Event date: 2022.6

    Language:Japanese   Presentation type:Oral presentation (general)  

    Country:Japan  

  • 血清環境における抗体の分子間相互作用と機能の解明

    與語理那, 谷中冴子, 矢木宏和, 加藤晃一

    日本薬学会年会要旨集(Web)  2021.3 

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  • High-precision structural analysis of antibody molecules by SEC-iCM-SANS

    佐藤信浩, 與語理那, 與語理那, 與語理那, 谷中冴子, 谷中冴子, 谷中冴子, MARTEL Anne, PORCAR Lionel, 守島健, 井上倫太郎, 富永大輝, 有森貴夫, 高木淳一, 杉山正明, 加藤晃一, 加藤晃一, 加藤晃一

    量子ビームサイエンスフェスタ(Web)  2021 

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  • 安定同位体標識を利用したNMRによる抗体の「品質」の解析

    谷中冴子, 谷中冴子, 與語理那, 與語理那, 矢木宏和, 加藤晃一, 加藤晃一

    日本分子生物学会年会プログラム・要旨集(Web)  2019.12 

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  • 抗体のNMR解析のための安定同位体標識法の開発と応用

    谷中冴子, 與語理那, 山崎俊夫, 宮ノ入洋平, 矢木宏和, 加藤晃一

    2019.11 

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  • 膜を舞台にする抗体機能の高速原子間力顕微鏡解析

    與語理那, 谷中冴子渡辺大輝, 矢木宏和, 内橋貴之, 加藤晃一

    日本薬学会年会要旨集(CD-ROM)  2019.3 

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  • IgGとFc受容体の相互作用におけるFab領域の新規結合部位の同定

    與語理那, 與語理那, 山口祐希, 渡辺大輝, 矢木宏和, 佐藤匡史, 中西真人, 鬼塚正義, 大政健史, 嶋田麻里, 丸野孝浩, 鳥巣哲生, 渡邊史生, 肥後大輔, 内橋貴之, 内橋貴之, 谷中冴子, 谷中冴子, 内山進, 内山進, 加藤晃一, 加藤晃一

    日本生化学会大会(Web)  2019.3 

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  • Fcの構造ダイナミクスがFcγ受容体との相互作用に及ぼす影響の解明

    谷中冴子, 谷中冴子, 谷中冴子, 與語理那, 與語理那, 與語理那, 矢木宏和, 伊藤暁, 伊藤暁, 奥村久士, 奥村久士, 加藤晃一, 加藤晃一, 加藤晃一

    日本薬学会年会要旨集(CD-ROM)  2019 

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  • IgGのフコシル化によるFcのダイナミクスの変化がFcγ受容体との相互作用に及ぼす影響

    谷中冴子, 谷中冴子, 谷中冴子, 谷中冴子, 與語理那, 與語理那, 與語理那, 矢木宏和, 伊藤暁, 伊藤暁, 伊藤暁, 奥村久士, 奥村久士, 奥村久士, 山口拓実, 加藤晃一, 加藤晃一, 加藤晃一, 加藤晃一

    日本細胞生物学会大会(Web)  2019 

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  • HDX-MSによる抗体とFc受容体の相互作用解析

    山口祐希, 與語理那, 與語理那, 矢木宏和, 佐藤匡史, 中西真人, 嶋田麻里, 丸野孝浩, 鳥巣哲生, 渡邊史生, 肥後大輔, 谷中冴子, 谷中冴子, 加藤晃一, 加藤晃一, 内山進, 内山進

    日本分子生物学会年会プログラム・要旨集(Web)  2019 

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  • 動的相互作用機構解析に基づいたレクチン高親和性糖鎖の設計

    中根健汰, 鈴木達哉, 谷中冴子, 加藤晃一, 山口拓実

    日本化学会春季年会講演予稿集(CD-ROM)  2019 

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  • 糖鎖コンフォメーション空間の改変による糖-タンパク質間相互作用の制御

    山口拓実, 山口拓実, 鈴木達哉, 龍岡博亮, 谷中冴子, 矢木宏和, 佐藤匡史, 加藤晃一, 加藤晃一

    ホスト-ゲスト・超分子化学シンポジウム講演要旨集  2019 

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  • 深海の化学合成生態系に優占する共生微生物の糖鎖生物学的性状

    土井昂大, 島村繁, 矢木宏和, 矢木真穂, 谷中冴子, 澤山茂樹, 井町寛之, 高井研, 高井研, 加藤晃一, 加藤晃一, 中川聡, 中川聡

    日本微生物生態学会大会(Web)  2019 

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    Event date: 2019

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  • 未結合状態の糖鎖のコンフォメーション空間の改変によるレクチン親和性の向上

    鈴木達哉, 鈴木達哉, 谷中冴子, 谷中冴子, 渡邉東紀男, YAN Gengwei, 佐藤匡史, 矢木宏和, 山口拓実, 加藤晃一, 加藤晃一

    日本糖質学会年会要旨集  2019 

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  • NMRと計算科学の統合による糖鎖の3次元構造ダイナミクスの解析

    矢木宏和, 鈴木達哉, 鈴木達哉, 谷中冴子, 谷中冴子, 山口拓実, 山口拓実, 加藤晃一, 加藤晃一

    バイオイメージング  2018 

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  • コンフォメーション空間の改変によるレクチン高親和性糖鎖の創成

    鈴木達哉, 鈴木達哉, 谷中冴子, 谷中冴子, 渡邉東紀男, YAN Gengwei, 佐藤匡史, 矢木宏和, 山口拓実, 加藤晃一, 加藤晃一

    日本糖質学会年会要旨集  2018 

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  • ヒト抗体軽鎖定常領域のNMR解析

    ソン ドクヨン, 谷中冴子, 谷中冴子, 與語理那, 與語理那, 矢木宏和, BOONSRI Pornthip, 加藤晃一, 加藤晃一

    日本病院薬剤師会東海ブロック・日本薬学会東海支部合同学術大会講演要旨集  2018 

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  • 解離会合平衡下にあるタンパク質会合体の構造解析

    守島健, 佐藤信浩, 井上倫太郎, 與語理那, 與語理那, 谷中冴子, 谷中冴子, 矢木宏和, 加藤晃一, 加藤晃一, 加藤晃一, MARTEL Anne, PORCAR Lionel, 杉山正明

    日本中性子科学会年会講演概要集  2018 

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  • 核磁気共鳴法と中性子小角散乱法によるFcとFc受容体の相互作用解析

    與語理那, 與語理那, 谷中冴子, 谷中冴子, 矢木宏和, 井上倫太郎, 杉山正明, 加藤晃一, 加藤晃一

    日本薬学会年会要旨集(CD-ROM)  2018 

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  • 核磁気共鳴法と中性子小角散乱法によるFcとFcγ受容体の相互作用解析

    與語理那, 與語理那, 谷中冴子, 谷中冴子, 矢木宏和, 井上倫太郎, 杉山正明, 加藤晃一, 加藤晃一

    Abstracts. Annual Meeting of the NMR Society of Japan  2018 

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  • 抗体研究から学ぶこと

    谷中冴子

    日本生化学会大会(Web)  2018 

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  • 抗体医薬の作動メカニズムの構造基盤

    谷中冴子, 與語理那, 矢木宏和, 加藤晃一, 加藤晃一

    日本薬学会年会要旨集(CD-ROM)  2018 

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  • 分子シャペロンによるモノグルコシル化糖鎖認識機構の解析

    中根健汰, 鈴木達哉, 谷中冴子, 加藤晃一, 山口拓実

    日本化学会春季年会講演予稿集(CD-ROM)  2018 

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  • NMRを用いた血清中での抗体の相互作用解析

    谷中冴子, 谷中冴子, 與語理那, 與語理那, 矢木宏和, 加藤晃一, 加藤晃一

    日本薬学会年会要旨集(CD-ROM)  2017 

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  • NMRを用いた血清中における抗体の相互作用解析

    谷中冴子, 谷中冴子, 谷中冴子, 與語理那, 與語理那, 與語理那, 矢木宏和, 加藤晃一, 加藤晃一, 加藤晃一, 加藤晃一

    日本蛋白質科学会年会プログラム・要旨集  2017 

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  • NMRを用いた血清中での抗体の相互作用解析

    谷中冴子, 谷中冴子, 山崎俊夫, 與語理那, 與語理那, 矢木宏和, 加藤晃一, 加藤晃一

    Abstracts. Annual Meeting of the NMR Society of Japan  2017 

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  • 機能制御を指向したルイスX糖鎖の動的立体構造解析と化学構造改変

    鈴木達哉, 鈴木達哉, YAN Gengwei, YAN Gengwei, 谷中冴子, 谷中冴子, 矢木宏和, 村上真吾, 堀由樹, 山口拓実, 山口拓実, 山口拓実, 加藤晃一, 加藤晃一

    日本糖質学会年会要旨集  2017 

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  • 高速原子間力顕微鏡で可視化するタンパク質の動的秩序

    内橋貴之, 杉山翔吾, 小財稔矢, 與語理那, 谷中冴子, 佐藤匡史, 矢木和宏, 盛徹也, JOHNSON Carl, 安藤敏夫, 加藤晃一, 加藤晃一

    日本蛋白質科学会年会プログラム・要旨集  2017 

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  • 高速AFMを用いた膜上での抗原抗体複合体形成過程の観測

    與語理那, 與語理那, 谷中冴子, 谷中冴子, 矢木宏和, 内橋貴之, 加藤晃一, 加藤晃一

    日本薬学会年会要旨集(CD-ROM)  2017 

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  • 自己組織化糖鎖クラスターを用いた糖鎖間相互作用による超分子会合体の形成

    山口拓実, 山口拓実, 山口拓実, YAN Gengwei, YAN Gengwei, 鈴木達哉, 鈴木達哉, 谷中冴子, 谷中冴子, 佐藤宗太, 藤田誠, 加藤晃一, 加藤晃一

    日本糖質学会年会要旨集  2017 

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  • グルコース残基を目印とした小胞体品質管理システムの構造的理解

    佐藤匡史, 佐藤匡史, ZHU Tong, ZHU Tong, 年森隆泰, 年森隆泰, 梶野愛, YAN Gengwei, YAN Gengwei, YAN Gengwei, 鈴木達哉, 鈴木達哉, 谷中冴子, 谷中冴子, 山口拓実, 山口拓実, 山口拓実, 上久保裕生, 内橋貴之, 加藤晃一, 加藤晃一, 加藤晃一, 加藤晃一

    日本糖質学会年会要旨集  2016 

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  • レプリカ交換分子動力学シミュレーションによる抗体及びFc受容体内の糖鎖分子の解析

    榮慶丈, 山口拓実, 佐藤匡史, 谷中冴子, 加藤晃一, 加藤晃一, 岡本祐幸

    生体分子科学討論会講演要旨集  2016 

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  • 化学-酵素合成法による安定同位体標識高マンノース型GM9糖鎖の調製とNMR立体構造解析

    鈴木達哉, 鈴木達哉, 梶野愛, ZHU Tong, ZHU Tong, ZHU Tong, 佐藤匡史, 谷中冴子, 谷中冴子, 山口拓実, 山口拓実, 山口拓実, 山口拓実, 加藤晃一, 加藤晃一, 加藤晃一

    日本糖質学会年会要旨集  2016 

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  • FcγIII受容体との相互作用における抗体のダイナミックな構造変化

    與語理那, 矢木宏和, 谷中冴子, 矢木真穂, 加藤晃一, 谷中冴子, 矢木真穂, 加藤晃一

    日本病院薬剤師会東海ブロック・日本薬学会東海支部合同学術大会講演要旨集  2015 

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  • NMRを用いたヒト主要組織適合複合体の動的なペプチド認識及び構造維持機構の解明

    谷中冴子, 上野貴将, YI Shi, YI Shi, QI Jianxun, QI Jianxun, GAO George, GAO George, 津本浩平, 津本浩平, 菅瀬謙治

    Abstracts. Annual Meeting of the NMR Society of Japan  2013 

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  • ヒト主要組織適合複合体の動的なペプチド認識および構造維持機構

    谷中冴子, 菅瀬謙治, 上野貴将, 津本浩平

    日本蛋白質科学会年会プログラム・要旨集  2013 

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  • ボトムアップ型構造体の構築を指向した重合性蛋白質モノマーの精密設計

    松長遼, 谷中冴子, 津本浩平

    日本化学会講演予稿集  2013 

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  • ヒト主要組織適合複合体の安定化機構に関する解析

    谷中冴子, 菅瀬謙治, 上野貴将, 津本浩平

    Abstracts. Annual Meeting of the NMR Society of Japan  2012 

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  • 還元環境下で自発的な共有結合形成により重合する蛋白質の開発

    松長遼, 谷中冴子, 中川一路, 津本浩平

    日本化学会講演予稿集  2012 

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  • 還元環境に応答して直列に重合する蛋白質の設計と解析

    松長遼, 松長遼, 谷中冴子, 谷中冴子, 中川一路, 津本浩平, 津本浩平

    高分子学会予稿集(CD-ROM)  2012 

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  • レンサ球菌の線毛構成蛋白質をもとにした自発的に還元環境下で重合する蛋白質の設計

    松長遼, 谷中冴子, 中川一路, 津本浩平, 津本浩平

    日本蛋白質科学会年会プログラム・要旨集  2012 

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  • ヒト主要組織適合複合体の揺らぎが安定性に与える影響について

    谷中冴子, 菅瀬謙治, 上野貴将, 津本浩平

    日本蛋白質科学会年会プログラム・要旨集  2012 

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  • ヒト主要組織適合複合体(HLA)の揺らぎが傷害性T細胞(CTL)に与える影響について

    谷中冴子, 菅瀬謙治, 上野貴将, 津本浩平

    日本蛋白質科学会年会プログラム・要旨集  2011 

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  • ヒト主要組織適合複合体の動的構造と傷害性T細胞の活性の関連について

    谷中冴子, 上野貴将, 本園千尋, 菅瀬謙治, 津本浩平

    日本蛋白質科学会年会プログラム・要旨集  2010 

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  • 蛋白質科学と病原性微生物:黄色ブドウ球菌由来蛋白質

    津本浩平, 田中良和, 工藤基徳, 中木戸誠, 渡邊正人, 安部良太, 宮房孝光, 谷中冴子, 森脇由隆

    日本蛋白質科学会年会プログラム・要旨集  2010 

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  • レンサ球菌由来線毛構成蛋白質のin vitro重合

    松長遼, 谷中冴子, 中川一路, 津本浩平

    日本蛋白質科学会年会プログラム・要旨集  2010 

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  • HLA-HIV由来抗原ペプチド複合体の熱安定性と抗原性

    谷中冴子, 本園千尋, 工藤基徳, 上野貴将, 津本浩平

    日本蛋白質科学会年会プログラム・要旨集  2009 

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  • T細胞レセプターのHIV抗原変異に対する交差反応性

    本園千尋, 谷中冴子, 津本浩平, 滝口雅文, 上野貴将

    日本蛋白質科学会年会プログラム・要旨集  2009 

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  • ワクチンの創成を目指した黄色ブドウ球菌毒素改変体の分子特性解析

    谷中冴子, 工藤基徳, 田中良和, 中島敏博, 津本浩平

    日本化学会バイオテクノロジー部会シンポジウム講演要旨集  2008 

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  • ワクチンの創製を目指した黄色ブドウ球菌毒素改変体の分子特性解析

    谷中冴子, 田中良和, 中島敏博, 津本浩平

    日本化学会講演予稿集  2008 

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  • ワクチンの創製を目指した黄色ブドウ球菌毒素改変体の分子特性解析

    谷中冴子, 田中良和, 中島敏博, 津本浩平

    日本蛋白質科学会年会プログラム・要旨集  2008 

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  • 6M塩化グアニジニウム中でアンフォールドした3ヘリックス・バンドル蛋白質の残存構造のH/D交換2次元NMRによる研究(Residual structures in the unfolded state in a three-helix-bundle protein in 6 M guanidinium chloride studied by H/D-exchange 2D NMR)

    Kuwajima Kunihiro, Yanaka Saeko, Yagi-Utsumi Maho, Kato Koichi

    生物物理  2022.8  (一社)日本生物物理学会

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  • ヘムと相互作用する化膿連鎖球菌由来鉄獲得蛋白質の構造基盤

    関 幹太, 妹尾 暁暢, 谷中 冴子, カアベイロ・ホセ

    日本生化学会大会プログラム・講演要旨集  2023.10  (公社)日本生化学会

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  • 情報計算科学にもとづく酵素の創成と応用~スーパー酵素が切り拓く生化学の新時代~ 構造ダイナミクスの観点からの抗体の機能解読と改変

    谷中 冴子, 加藤 晃一

    日本生化学会大会プログラム・講演要旨集  2023.10  (公社)日本生化学会

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MISC

  • 抗体医薬の作動メカニズムの分子基盤 Reviewed

    谷中冴子、加藤晃一

    2023.7

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  • 【日本抗体学会設立記念特集~アカデミアと産業界の協力による日本の抗体研究への期待】抗体医薬の作動メカニズムの分子基盤

    谷中 冴子, 加藤 晃一

    生物工学会誌   101 ( 7 )   347 - 349   2023.7   ISSN:0919-3758

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  • 抗体医薬の作動メカニズムの分子基盤

    谷中冴子, 谷中冴子, 谷中冴子, 加藤晃一, 加藤晃一

    生物工学会誌   101 ( 7 )   2023   ISSN:0919-3758

  • Regulatory mechanism of protein glycosylation by passport sequence

    中野里音, 山田梨乃, 西栄美子, 斎藤泰輝, 犬塚健剛, 足達俊吾, 戸島拓郎, 古川潤一, 本田怜奈, 谷中冴子, 谷中冴子, 矢木真穂, 矢木真穂, 矢木宏和, 矢木宏和, 加藤晃一, 加藤晃一

    日本薬学会年会要旨集(Web)   143rd   2023   ISSN:0918-9823

  • 最先端基盤技術 II.タンパク質工学と抗体医薬 8.抗体のエフェクター活性と定常部を介した抗体の高機能化 Reviewed

    谷中冴子、加藤晃一

    2022.12

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  • 【治療の可能性が広がる 抗体医薬 バイスペシフィック抗体、ADC、シングルドメイン抗体、機械学習…新技術と情報科学が実現した新時代のモダリティ】(第1章)最先端基盤技術 タンパク質工学と抗体医薬 抗体のエフェクター活性と定常部を介した抗体の高機能化

    加藤 晃一, 谷中 冴子

    実験医学   40 ( 20 )   3253 - 3258   2022.12   ISSN:0288-5514

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    Fcγ受容体をはじめとするエフェクター分子は抗体のFc領域の共通部位に結合する.抗体医薬の高機能化においてこうした部位を標的とした分子改変が進められている.一方,Fc領域は糖鎖修飾を受けており,糖鎖の構造がエフェクター機能に大きな影響を与える.さらに最近の研究により,抗体分子の定常部にエフェクター分子との相互作用を規定する部位が新たに見出されており,分子中に張り巡らされたアロステリックネットワークの存在も浮き彫りになってきた.こうした知見は,抗体の高機能化に重要な示唆を与える.(著者抄録)

  • Antibody effector functions and functional improvement of antibodies via their constant regions

    加藤晃一, 加藤晃一, 谷中冴子, 谷中冴子

    実験医学   40 ( 20 )   2022   ISSN:0288-5514

  • 核磁気共鳴分光法と分子動力学計算を通じて観る糖鎖の動的構造とレクチンの糖鎖認識の理解 (第1土曜特集 レクチン医学最前線) -- (レクチン-糖鎖相互作用の物理化学的理解)

    矢木 宏和, 鈴木 達哉, 谷中 冴子, 山口 拓実, 加藤 晃一

    医学のあゆみ   2019.6

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  • 抗体のNMR研究の趨向と展望

    加藤晃一, 谷中冴子

    2018.10

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  • NMRと計算科学の統合による糖鎖の3次元構造ダイナミクスの解析

    矢木宏和, 鈴木達哉, 鈴木達哉, 谷中冴子, 谷中冴子, 山口拓実, 山口拓実, 加藤晃一, 加藤晃一

    バイオイメージング   2018.8

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  • The Dynamic Peptide Recognition And Stabilization Mechanism Of Human Leukocyte Antigen B*35:01

    Saeko Yanaka, Takamasa Ueno, Kouhei Tsumoto, Kenji Sugase

    PROTEIN SCIENCE   2014.7

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  • 若手の会によるフォーラム開催の報告

    谷中 冴子, 飯島 玲生

    生化學   2012.5

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  • Isothiocyanate blocks restitution and wound repair in the mammalian stomach by inhibiting both monocarboxylate and bicarbonate transport activity

    Regina Ragasa, Eiji Nakamura, Lisa M. Marrone, Saeko Yanaka, Shusaku Hayashi, Koji Takeuchi, Susan J. Hagen

    GASTROENTEROLOGY   2007.4

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Professional Memberships

  • THE JAPANESE BIOCHEMICAL SOCIETY

  • THE BIOPHYSICAL SOCIETY OF JAPAN

  • THE PHARMACEUTICAL SOCIETY OF JAPAN

  • PROTEIN SCIENCE SOCIETY OF JAPAN

  • 日本核磁気共鳴学会

  • PROTEIN SCIENCE SOCIETY OF JAPAN

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  • THE PHARMACEUTICAL SOCIETY OF JAPAN

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  • THE BIOPHYSICAL SOCIETY OF JAPAN

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  • 日本核磁気共鳴学会

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Committee Memberships

  • 日本核磁気共鳴学会   評議員  

    2022.11 - 2023.10   

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  • 日本蛋白質科学会   理事  

    2022.6 - 2026.6   

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  • Executive   Domestic

    2022.6 - 2024.6   

  • 日本生物物理学会   代議員  

    2021.9 - 2024.8   

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  • 日本生物物理学会   代議員   Domestic

    2021.6 - 2025.6   

Academic Activities

  • 実行委員

    第61回日本生物物理学会年会  2023.11

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    Type:Competition, symposium, etc. 

  • 募金委員 International contribution

    2021.8

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    Type:Competition, symposium, etc. 

Research Projects

  • 実験科学と情報科学の融合によるバイオ医薬品設計の技術開発

    2023 - 2025

    日本医療研究開発機構(AMED) 創薬基盤推進研究事業

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    Authorship:Principal investigator  Grant type:Contract research

  • 物質-生命の境界探査

    2022.9 - 2027.3

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    Authorship:Collaborating Investigator(s) (not designated on Grant-in-Aid) 

  • Deciphering the molecular meridians of antibodies to improve the functionality of antibody drugs

    Grant number:23K24018  2022.4 - 2026.3

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

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    Authorship:Principal investigator  Grant type:Scientific research funding

    CiNii Research

  • 抗体医薬の高機能化に向けた抗体の分子経絡の解読と改変

    Grant number:22H02755  2022 - 2025

    日本学術振興会  科学研究費助成事業  基盤研究(B)

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    Grant type:Scientific research funding

  • 分子中に秘められた新規相互作用部位の探査と改変を通じた次世代抗体創成の基盤構築

    2021 - 2025

    日本医療研究開発機構(AMED)次世代治療・診断実現のための創薬基盤技術開発 国際競争力のある次世代抗体医薬品製造技術開発

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    Authorship:Principal investigator  Grant type:Contract research

  • 糖鎖とタンパク質が織りなす抗体のアロステリックネットワークの探査

    2020 - 2021

    日本学術振興会  科学研究費助成事業  若手研究

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    Authorship:Principal investigator  Grant type:Scientific research funding

  • 先端計測アプローチの統合による抗体の構造動態と機能発現の連関機構の解明

    Grant number:19H01017  2019 - 2022

    日本学術振興会  科学研究費助成事業  基盤研究(A)

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    Grant type:Scientific research funding

  • 抗体とFc受容体の新規相互作用様式の解明と抗体工学への展開

    2018 - 2019

    日本学術振興会  科学研究費助成事業  若手研究

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    Authorship:Principal investigator  Grant type:Scientific research funding

  • 抗体の分子認識を契機とする補体系の活性化を活写する

    2017 - 2018

    日本学術振興会・文部科学省  科学研究費助成事業  新学術領域研究

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    Authorship:Principal investigator  Grant type:Scientific research funding

  • 多元的構造生物学アプローチによるプロテアソーム形成機構の解明と創薬への展開

    Grant number:15H02491  2015 - 2018

    日本学術振興会  科学研究費助成事業  基盤研究(A)

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    Grant type:Scientific research funding

  • 生命分子の動的秩序形成におけるミクロ‐マクロ相関の探査と設計原理の探求

    Grant number:25102008  2013 - 2017

    日本学術振興会・文部科学省  科学研究費助成事業  新学術領域研究

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    Grant type:Scientific research funding

  • 抗原抗体相互作用の動的構造解析を基盤とした高機能抗体の設計

    2013 - 2015

    日本学術振興会  科学研究費助成事業  特別研究員奨励費

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    Authorship:Principal investigator  Grant type:Scientific research funding

  • ヒト主要組織適合複合体の揺らぎと細胞の抗原提示能に関する研究

    Grant number:11J06193  2011 - 2012

    日本学術振興会  科学研究費助成事業  特別研究員奨励費

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    Authorship:Principal investigator  Grant type:Scientific research funding

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Class subject

  • 生命薬学IB

    2024.10 - 2025.3   Second semester

  • 生命薬学IA

    2024.4 - 2024.9   First semester

  • 生命薬学IB

    2023.10 - 2024.3   Second semester

  • 生命薬学IA

    2023.4 - 2023.9   First semester

  • 創薬科学総論III

    2022.4 - 2022.9   First semester

  • 生命薬学ⅠB

    2024.10 - 2024.12   Fall quarter

  • 生命薬学ⅠA

    2024.4 - 2024.6   Spring quarter

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FD Participation

  • 2023.11   Role:Planning   Title:第2回薬学部局FD講演会「機関間連携」

    Organizer:[Undergraduate school/graduate school/graduate faculty]

  • 2023.8   Role:Planning   Title:男女共同参画FD

    Organizer:[Undergraduate school/graduate school/graduate faculty]

Visiting, concurrent, or part-time lecturers at other universities, institutions, etc.

  • 2023  自然科学研究機構 生命創成探究センター  Classification:Part-time faculty  Domestic/International Classification:Japan 

  • 2023  鹿児島大学理学部  Classification:Part-time lecturer  Domestic/International Classification:Japan 

  • 2022  自然科学研究機構 生命創成探究センター/分子科学研究所  Classification:Part-time faculty  Domestic/International Classification:Japan 

Other educational activity and Special note

  • 2023  Class Teacher 

Outline of Social Contribution and International Cooperation activities

  • グローバルヘルスケア分野を通じた社会貢献・国際連携活動