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齋尾智英

徳島大学

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2024年11月15日更新

職名: 教授
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電子メール: saio@tokushima-u.ac.jp
学歴: 研究者総覧に該当データはありませんでした。
学位: 博士(生命科学) (北海道大学) (2011年3月)
職歴・経歴: 2020/9: 徳島大学教授, 先端酵素学研究所

専門分野・研究分野: 生物物理学 (Biophysics)

研究者総覧で最新データを確認する

2024年11月15日更新

専門分野・研究分野: 生物物理学 (Biophysics)
担当経験のある授業科目: プロテオミクス概論
医学科2年令和5年度生化学
指導経験: 1人 (修士)

研究者総覧で最新データを確認する

2024年11月15日更新

専門分野・研究分野: 生物物理学 (Biophysics)

研究テーマ: 生命恒常性維持の分子メカニズム解明

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論文

Saori Yoshimura, Ryuki Shimada, Koji Kikuchi, Soichiro Kawagoe, Hironori Abe, Sakie Iisaka, Sayoko Fujimura, Kei-Ichiro Yasunaga, Shingo Usuki, Naoki Tani, Takashi Ohba, Eiji Kondoh, Tomohide Saio, Kimi Araki and Kei-Ichiro Ishiguro :
Atypical heat shock transcription factor HSF5 is critical for male meiotic prophase under non-stress conditions.,
Nature Communications, Vol.15, No.1, 3330, 2024.

(要約): Meiotic prophase progression is differently regulated in males and females. In males, pachytene transition during meiotic prophase is accompanied by robust alteration in gene expression. However, how gene expression is regulated differently to ensure meiotic prophase completion in males remains elusive. Herein, we identify HSF5 as a male germ cell-specific heat shock transcription factor (HSF) for meiotic prophase progression. Genetic analyzes and single-cell RNA-sequencing demonstrate that HSF5 is essential for progression beyond the pachytene stage under non-stress conditions rather than heat stress. Chromatin binding analysis in vivo and DNA-binding assays in vitro suggest that HSF5 binds to promoters in a subset of genes associated with chromatin organization. HSF5 recognizes a DNA motif different from typical heat shock elements recognized by other canonical HSFs. This study suggests that HSF5 is an atypical HSF that is required for the gene expression program for pachytene transition during meiotic prophase in males.
(キーワード): Female / Male / Mice / Heat Shock Transcription Factors / Heat-Shock Response / Meiotic Prophase I / Mice, Inbred C57BL / Mice, Knockout / Spermatogenesis / Testis / Animals
(出版サイトへのリンク): ● Publication site (DOI): 10.1038/s41467-024-47601-0
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 38684656; ● Search Scopus @ Elsevier (PMID): 38684656; ● Search Scopus @ Elsevier (DOI): 10.1038/s41467-024-47601-0

(DOI: 10.1038/s41467-024-47601-0, PubMed: 38684656) Takahiro Muraoka, Masaki Okumura and Tomohide Saio :
Enzymatic and synthetic regulation of polypeptide folding.,
Chemical Science, Vol.15, No.7, 2282-2299, 2024.

(要約): Proper folding is essential for the biological functions of all proteins. The folding process is intrinsically error-prone, and the misfolding of a polypeptide chain can cause the formation of toxic aggregates related to pathological outcomes such as neurodegenerative disease and diabetes. Chaperones and some enzymes are involved in the cellular proteostasis systems that assist polypeptide folding to diminish the risk of aggregation. Elucidating the molecular mechanisms of chaperones and related enzymes is important for understanding proteostasis systems and protein misfolding- and aggregation-related pathophysiology. Furthermore, mechanistic studies of chaperones and related enzymes provide important clues to designing chemical mimics, or chemical chaperones, that are potentially useful for recovering proteostasis activities as therapeutic approaches for treating and preventing protein misfolding-related diseases. In this Perspective, we provide a comprehensive overview of the latest understanding of the folding-promotion mechanisms by chaperones and oxidoreductases and recent progress in the development of chemical mimics that possess activities comparable to enzymes, followed by a discussion of future directions.
(出版サイトへのリンク): ● Publication site (DOI): 10.1039/d3sc05781j
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 38362427; ● Search Scopus @ Elsevier (PMID): 38362427; ● Search Scopus @ Elsevier (DOI): 10.1039/d3sc05781j

(DOI: 10.1039/d3sc05781j, PubMed: 38362427) Honoka Kawamukai, Shumpei Takishita, Kazumi Shimizu, Daisuke Kohda, Koichiro Ishimori and Tomohide Saio :
Conformational Distribution of a Multidomain Protein Measured by Single-Pair Small-Angle X-ray Scattering.,
The Journal of Physical Chemistry Letters, Vol.15, No.3, 744-750, 2024.

(要約): The difficulty in evaluating the conformational distribution of proteins in solution often hinders mechanistic insights. One possible strategy for visualizing conformational distribution is distance distribution measurement by single-pair small-angle X-ray scattering (SAXS), in which the scattering interference from only a specific pair of atoms in the target molecule is extracted. Despite this promising concept, with few applications in synthetic small molecules and DNA, technical difficulties have prevented its application in protein conformational studies. This study used a synthetic tag to fix the lanthanide ion at desired sites on the protein and used single-pair SAXS with contrast matching to evaluate the conformational distribution of the multidomain protein enzyme MurD. These data highlighted the broad conformational and ligand-driven distribution shifts of MurD in solution. This study proposes an important strategy in solution structural biology that targets dynamic proteins, including multidomain and intrinsically disordered proteins.
(キーワード): Scattering, Small Angle / X-Rays / X-Ray Diffraction / Protein Conformation / Intrinsically Disordered Proteins
(出版サイトへのリンク): ● Publication site (DOI): 10.1021/acs.jpclett.3c02600
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 38221741; ● Summary page in Scopus @ Elsevier: 2-s2.0-85183335561

(DOI: 10.1021/acs.jpclett.3c02600, PubMed: 38221741, Elsevier: Scopus) Sachiho Taniguchi, Yuji Ono, Yukako Doi, Shogo Taniguchi, Yuta Matsuura, Ayuka Iwasaki, Noriaki Hirata, Ryosuke Fukuda, Keitaro Inoue, Miho Yamaguchi, Anju Tashiro, Daichi Egami, Shunsuke Aoki, Yasumitsu Kondoh, Kaori Honda, Hiroyuki Osada, Hiroyuki Kumeta, Tomohide Saio and Tsukasa Okiyoneda :
Identification of α-Tocopherol succinate as an RFFL-substrate interaction inhibitor inducing peripheral CFTR stabilization and apoptosis,
Biochemical Pharmacology, Vol.215, 115730, 2023.

(要約): The E3 ubiquitin ligase RFFL is an apoptotic inhibitor highly expressed in cancers and its knockdown suppresses cancer cell growth and sensitizes to chemotherapy. RFFL also participates in peripheral protein quality control which removes the functional cell surface ΔF508-CFTR channel and reduces the efficacy of pharmaceutical therapy for cystic fibrosis (CF). Although RFFL inhibitors have therapeutic potential for both cancer and CF, they remain undiscovered. Here, a chemical array screening has identified α-tocopherol succinate (αTOS) as an RFFL ligand. NMR analysis revealed that αTOS directly binds to RFFL's substrate-binding region without affecting the E3 enzymatic activity. Consequently, αTOS inhibits the RFFL-substrate interaction, ΔF508-CFTR ubiquitination and elimination from the plasma membrane of epithelial cells, resulting in the increased functional CFTR channel. Among the α-tocopherol (αTOL) analogs we tested, only αTOS inhibited the RFFL-substrate interaction and increased the cell surface ΔF508-CFTR, depending on RFFL expression. Similarly, the unique proapoptotic effect of αTOS was dependent on RFFL expression. Thus, unlike other αTOL analogs, αTOS acts as an RFFL protein-protein interaction inhibitor which may explain its unique biological properties among αTOL analogs. Moreover, αTOS may act as a CFTR stabilizer, a novel class of drugs that extend cell surface ΔF508-CFTR lifetime.
(キーワード): Humans / alpha-Tocopherol / Cystic Fibrosis Transmembrane Conductance Regulator / Antioxidants / Cystic Fibrosis / Apoptosis
(出版サイトへのリンク): ● Publication site (DOI): 10.1016/j.bcp.2023.115730
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 37543348; ● Summary page in Scopus @ Elsevier: 2-s2.0-85166771277

(DOI: 10.1016/j.bcp.2023.115730, PubMed: 37543348, Elsevier: Scopus) Soichiro Kawagoe, Munehiro Kumashiro, Takuya Mabuchi, Hiroyuki Kumeta, Koichiro Ishimori and Tomohide Saio :
Heat-Induced Conformational Transition Mechanism of Heat Shock Factor 1 Investigated by Tryptophan Probe.,
Biochemistry, Vol.61, No.24, 2897-2908, 2022.

(要約): A transcriptional regulatory system called heat shock response (HSR) has been developed in eukaryotic cells to maintain proteome homeostasis under various stresses. Heat shock factor-1 (Hsf1) plays a central role in HSR, mainly by upregulating molecular chaperones as a transcription factor. Hsf1 forms a complex with chaperones and exists as a monomer in the resting state under normal conditions. However, upon heat shock, Hsf1 is activated by oligomerization. Thus, oligomerization of Hsf1 is considered an important step in HSR. However, the lack of information about Hsf1 monomer structure in the resting state, as well as the structural change via oligomerization at heat response, impeded the understanding of the thermosensing mechanism through oligomerization. In this study, we applied solution biophysical methods, including fluorescence spectroscopy, nuclear magnetic resonance, and circular dichroism spectroscopy, to investigate the heat-induced conformational transition mechanism of Hsf1 leading to oligomerization. Our study showed that Hsf1 forms an inactive closed conformation mediated by intramolecular contact between leucine zippers (LZs), in which the intermolecular contact between the LZs for oligomerization is prevented. As the temperature increases, Hsf1 changes to an open conformation, where the intramolecular LZ interaction is dissolved so that the LZs can form intermolecular contacts to form oligomers in the active form. Furthermore, since the interaction sites with molecular chaperones and nuclear transporters are also expected to be exposed in the open conformation, the conformational change to the open state can lead to understanding the regulation of Hsf1-mediated stress response through interaction with multiple cellular components.
(キーワード): DNA-Binding Proteins / Heat Shock Transcription Factors / Tryptophan / Molecular Chaperones / Heat-Shock Response
(出版サイトへのリンク): ● Publication site (DOI): 10.1021/acs.biochem.2c00492
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 36485006; ● Search Scopus @ Elsevier (PMID): 36485006; ● Search Scopus @ Elsevier (DOI): 10.1021/acs.biochem.2c00492

(DOI: 10.1021/acs.biochem.2c00492, PubMed: 36485006) Masato Miyake, Mitsuaki Sobajima, Kiyoe Kurahashi, Akira Shigenaga, Masaya Denda, Akira Otaka, Tomohide Saio, Naoki Sakane, Hidetaka Kosako and Seiichi Oyadomari :
Identification of an endoplasmic reticulum proteostasis modulator that enhances insulin production in pancreatic β cells.,
Cell Chemical Biology, Vol.29, No.6, 996-1009.e9, 2022.

(要約): Perturbation of endoplasmic reticulum (ER) proteostasis is associated with impairment of cellular function in diverse diseases, especially the function of pancreatic β cells in type 2 diabetes. Restoration of ER proteostasis by small molecules shows therapeutic promise for type 2 diabetes. Here, using cell-based screening, we report identification of a chemical chaperone-like small molecule, KM04794, that alleviates ER stress. KM04794 prevented protein aggregation and cell death caused by ER stressors and a mutant insulin protein. We also found that this compound increased intracellular and secreted insulin levels in pancreatic β cells. Chemical biology and biochemical approaches revealed that the compound accumulated in the ER and interacted directly with the ER molecular chaperone BiP. Our data show that this corrector of ER proteostasis can enhance insulin storage and pancreatic β cell function.
(キーワード): Diabetes Mellitus, Type 2 / Endoplasmic Reticulum / Endoplasmic Reticulum Stress / Humans / Insulin / Insulin-Secreting Cells / Proteostasis / Unfolded Protein Response
(徳島大学機関リポジトリ): ● Metadata: 116761
(出版サイトへのリンク): ● Publication site (DOI): 10.1016/j.chembiol.2022.01.002
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 35143772; ● Search Scopus @ Elsevier (PMID): 35143772; ● Search Scopus @ Elsevier (DOI): 10.1016/j.chembiol.2022.01.002

(徳島大学機関リポジトリ: 116761, DOI: 10.1016/j.chembiol.2022.01.002, PubMed: 35143772) Motonori Matsusaki, Rina Okada, Yuya Tanikawa, Shingo Kanemura, Dai Ito, Yuxi Lin, Mai Watabe, Hiroshi Yamaguchi, Tomohide Saio, Young-Ho Lee, Kenji Inaba and Masaki Okumura :
Functional Interplay between P5 and PDI/ERp72 to Drive Protein Folding,
Biology, Vol.10, No.11, 1112, 2021.

(要約): The physiological functions of proteins are destined by their unique three-dimensional structures. Almost all biological kingdoms share conserved disulfide-catalysts and chaperone networks that assist in correct protein folding and prevent aggregation. Disruption of these networks is implicated in pathogenesis, including neurodegenerative disease. In the mammalian endoplasmic reticulum (ER), more than 20 members of the protein disulfide isomerase family (PDIs) are believed to cooperate in the client folding pathway, but it remains unclear whether complex formation among PDIs via non-covalent interaction is involved in regulating their enzymatic and chaperone functions. Herein, we report novel functional hetero complexes between PDIs that promote oxidative folding and inhibit aggregation along client folding. The findings provide insight into the physiological significance of disulfide-catalyst and chaperone networks and clues for understanding pathogenesis associated with disruption of the networks.
(キーワード): protein disulfide isomerase family / disulfide bond / 小胞体 (endoplasmic reticulum) / oxidative folding / 分子シャペロン (molecular chaperone) / protein-protein interaction
(徳島大学機関リポジトリ): ● Metadata: 116440
(出版サイトへのリンク): ● Publication site (DOI): 10.3390/biology10111112
(文献検索サイトへのリンク): ● CiNii @ 国立情報学研究所 (CRID): 1050571547625565952; ● Summary page in Scopus @ Elsevier: 2-s2.0-85118999409

(徳島大学機関リポジトリ: 116440, DOI: 10.3390/biology10111112, CiNii: 1050571547625565952, Elsevier: Scopus) Haojie Zhu, Motonori Matsusaki, Taiga Sugawara, Koichiro Ishimori and Tomohide Saio :
Zinc-Dependent Oligomerization of Thermus thermophilus Trigger Factor Chaperone,
Biology, Vol.10, No.11, 1106, 2021.

(要約): Thermus thermophilus trigger factor (TtTF) is a zinc-dependent molecular chaperone whose folding-arrest activity is regulated by Zn2+. However, little is known about the mechanism of zinc-dependent regulation of the TtTF activity. Here we exploit in vitro biophysical experiments to investigate zinc-binding, the oligomeric state, the secondary structure, and the thermal stability of TtTF in the absence and presence of Zn2+. The data show that full-length TtTF binds Zn2+, but the isolated domains and tandem domains of TtTF do not bind to Zn2+. Furthermore, circular dichroism (CD) and nuclear magnetic resonance (NMR) spectra suggested that Zn2+-binding induces the partial structural changes of TtTF, and size exclusion chromatography-multi-angle light scattering (SEC-MALS) showed that Zn2+ promotes TtTF oligomerization. Given the previous work showing that the activity regulation of E. coli trigger factor is accompanied by oligomerization, the data suggest that TtTF exploits zinc ions to induce the structural change coupled with the oligomerization to assemble the client-binding site, thereby effectively preventing proteins from misfolding in the thermal environment.
(徳島大学機関リポジトリ): ● Metadata: 117166
(出版サイトへのリンク): ● Publication site (DOI): 10.3390/biology10111106
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 34827099; ● Search Scopus @ Elsevier (PMID): 34827099; ● Search Scopus @ Elsevier (DOI): 10.3390/biology10111106

(徳島大学機関リポジトリ: 117166, DOI: 10.3390/biology10111106, PubMed: 34827099) Hitoki Nanaura, Honoka Kawamukai, Ayano Fujiwara, Takeru Uehara, Yuichiro Aiba, Mari Nakanishi, Tomo Shiota, Masaki Hibino, Pattama Wiriyasermkul, Sotaro Kikuchi, Riko Nagata, Masaya Matsubayashi, Yoichi Shinkai, Tatsuya Niwa, Taro Mannen, Naritaka Morikawa, Naohiko Iguchi, Takao Kiriyama, Ken Morishima, Rintaro Inoue, Masaaki Sugiyama, Takashi Oda, Noriyuki Kodera, Sachiko Toma-Fukai, Mamoru Sato, Hideki Taguchi, Shushi Nagamori, Osami Shoji, Koichiro Ishimori, Hiroyoshi Matsumura, Kazuma Sugie, Tomohide Saio, Takuya Yoshizawa and Eiichiro Mori :
C9orf72-derived arginine-rich poly-dipeptides impede phase modifiers,
Nature Communications, Vol.12, No.1, 5301, 2021.

(要約): Nuclear import receptors (NIRs) not only transport RNA-binding proteins (RBPs) but also modify phase transitions of RBPs by recognizing nuclear localization signals (NLSs). Toxic arginine-rich poly-dipeptides from C9orf72 interact with NIRs and cause nucleocytoplasmic transport deficit. However, the molecular basis for the toxicity of arginine-rich poly-dipeptides toward NIRs function as phase modifiers of RBPs remains unidentified. Here we show that arginine-rich poly-dipeptides impede the ability of NIRs to modify phase transitions of RBPs. Isothermal titration calorimetry and size-exclusion chromatography revealed that proline:arginine (PR) poly-dipeptides tightly bind karyopherin-β2 (Kapβ2) at 1:1 ratio. The nuclear magnetic resonances of Kapβ2 perturbed by PR poly-dipeptides partially overlapped with those perturbed by the designed NLS peptide, suggesting that PR poly-dipeptides target the NLS binding site of Kapβ2. The findings offer mechanistic insights into how phase transitions of RBPs are disabled in C9orf72-related neurodegeneration.
(キーワード): Active Transport, Cell Nucleus / Binding Sites / C9orf72 Protein / Cloning, Molecular / DNA-Binding Proteins / Escherichia coli / Gene Expression / Genetic Vectors / HeLa Cells / Humans / Models, Molecular / Nuclear Localization Signals / Peptides / Phase Transition / Protein Binding / Protein Conformation / Protein Interaction Domains and Motifs / RNA-Binding Protein FUS / Recombinant Proteins / beta Karyopherins
(徳島大学機関リポジトリ): ● Metadata: 117572
(出版サイトへのリンク): ● Publication site (DOI): 10.1038/s41467-021-25560-0
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 34489423; ● Summary page in Scopus @ Elsevier: 2-s2.0-85114646807

(徳島大学機関リポジトリ: 117572, DOI: 10.1038/s41467-021-25560-0, PubMed: 34489423, Elsevier: Scopus) Hiroshi Nakagawa, Tomohide Saio, Michihiro Nagao, Rintaro Inoue, Masaaki Sugiyama, Satoshi Ajito, Taiki Tominaga and Yukinobu Kawakita :
Conformational dynamics of a multidomain protein by neutron scattering and computational analysis.,
Biophysical Journal, Vol.120, No.16, 3341-3354, 2021.

(要約): The flexible conformations of a multidomain protein are responsible for its biological functions. Although MurD, a 47-kDa protein that consists of three domains, sequentially changes its domain conformation from an open form to a closed form through a semiclosed form in its enzymatic reaction, the domain dynamics in each conformation remains unclear. In this study, we verify the conformational dynamics of MurD in the corresponding three states (apo and ATP- and inhibitor-bound states) with a combination of small-angle x-ray and neutron scattering (SAXS and SANS), dynamic light scattering (DLS), neutron backscattering (NBS), neutron spin echo (NSE) spectroscopy, and molecular dynamics (MD) simulations. Applying principal component analysis of the MD trajectories, twisting and open-closed domain modes are identified as the major collective coordinates. The deviations of the experimental SAXS profiles from the theoretical calculations based on the known crystal structures become smaller in the ATP-bound state than in the apo state, and a further decrease is evident upon inhibitor binding. These results suggest that domain motions of the protein are suppressed step by step of each ligand binding. The DLS and NBS data yield collective and self-translational diffusion constants, respectively, and we used them to extract collective domain motions in nanometer and nanosecond scales from the NSE data. In the apo state, MurD shows both twisting and open-closed domain modes, whereas an ATP binding suppresses twisting domain motions, and a further reduction of open-closed mode is seen in the inhibitor-binding state. These observations are consistent with the structure modifications measured by the small-angle scattering as well as the MD simulations. Such changes in the domain dynamics associated with the sequential enzymatic reactions should be related to the affinity and reaction efficiency with a ligand that binds specifically to each reaction state.
(出版サイトへのリンク): ● Publication site (DOI): 10.1016/j.bpj.2021.07.001
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 34242590; ● Search Scopus @ Elsevier (PMID): 34242590; ● Search Scopus @ Elsevier (DOI): 10.1016/j.bpj.2021.07.001

(DOI: 10.1016/j.bpj.2021.07.001, PubMed: 34242590) Tomohide Saio, Soya Hiramatsu, Mizue Asada, Hiroshi Nakagawa, Kazumi Shimizu, Hiroyuki Kumeta, Toshikazu Nakamura and Koichiro Ishimori :
electron paramagnetic resonance.,
Biophysical Journal, Vol.120, No.15, 2943-2951, 2021.

(要約): Despite their importance in function, the conformational state of proteins and its changes are often poorly understood, mainly because of the lack of an efficient tool. MurD, a 47-kDa protein enzyme responsible for peptidoglycan biosynthesis, is one of those proteins whose conformational states and changes during their catalytic cycle are not well understood. Although it has been considered that MurD takes a single conformational state in solution as shown by a crystal structure, the solution nuclear magnetic resonance (NMR) study suggested the existence of multiple conformational state of apo MurD in solution. However, the conformational distribution has not been evaluated. In this work, we investigate the conformational states of MurD by the use of electron paramagnetic resonance (EPR), especially intergadolinium distance measurement using double electron-electron resonance (DEER) measurement. The gadolinium ions are fixed on specific positions on MurD via a rigid double-arm paramagnetic lanthanide tag that has been originally developed for paramagnetic NMR. The combined use of NMR and EPR enables accurate interpretation of the DEER distance information to the structural information of MurD. The DEER distance measurement for apo MurD shows a broad distance distribution, whereas the presence of the inhibitor narrows the distance distribution. The results suggest that MurD exists in a wide variety of conformational states in the absence of ligands, whereas binding of the inhibitor eliminates variation in conformational states. The multiple conformational states of MurD were previously implied by NMR experiments, but our DEER data provided structural characterization of the conformational variety of MurD.
(キーワード): Electron Spin Resonance Spectroscopy / Ligands / Magnetic Resonance Spectroscopy / Molecular Conformation / Proteins
(出版サイトへのリンク): ● Publication site (DOI): 10.1016/j.bpj.2021.06.033
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 34242587; ● Search Scopus @ Elsevier (PMID): 34242587; ● Search Scopus @ Elsevier (DOI): 10.1016/j.bpj.2021.06.033

(DOI: 10.1016/j.bpj.2021.06.033, PubMed: 34242587) Masahiro Mimura, Shunsuke Tomita, Yoichi Shinkai, Takuya Hosokai, Hiroyuki Kumeta, Tomohide Saio, Kentaro Shiraki and Ryoji Kurita :
Quadruplex Folding Promotes the Condensation of Linker Histones and DNAs via Liquid-Liquid Phase Separation.,
Journal of the American Chemical Society, Vol.143, No.26, 9849-9857, 2021.

(要約): Liquid-liquid phase separation (LLPS) of proteins and DNA has recently emerged as a possible mechanism underlying the dynamic organization of chromatin. We herein report the role of DNA quadruplex folding in liquid droplet formation via LLPS induced by interactions between DNA and linker histone H1 (H1), a key regulator of chromatin organization. Fluidity measurements inside the droplets, binding assays using G-quadruplex-selective probes, and structural analyses based on circular dichroism demonstrated that quadruplex DNA structures, such as the G-quadruplex and i-motif, promote droplet formation with H1 and decrease molecular motility within droplets. The dissolution of the droplets in the presence of additives and the LLPS of the DNA structural units indicated that, in addition to electrostatic interactions between the DNA and the intrinsically disordered region of H1, π-π stacking between quadruplex DNAs could potentially drive droplet formation, unlike in the electrostatically driven LLPS of duplex DNA and H1. According to phase diagrams of anionic molecules with various conformations, the high LLPS ability associated with quadruplex folding arises from the formation of interfaces consisting of organized planes of guanine bases and the side surfaces with a high charge density. Given that DNA quadruplex structures are well-documented in heterochromatin regions, it is imperative to understand the role of DNA quadruplex folding in the context of intranuclear LLPS.
(出版サイトへのリンク): ● Publication site (DOI): 10.1021/jacs.1c03447
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 34152774; ● Search Scopus @ Elsevier (PMID): 34152774; ● Search Scopus @ Elsevier (DOI): 10.1021/jacs.1c03447

(DOI: 10.1021/jacs.1c03447, PubMed: 34152774) Masaki Okumura, Shingo Kanemura, Motonori Matsusaki, Misaki Kinoshita, Tomohide Saio, Dai Ito, Chihiro Hirayama, Hiroyuki Kumeta, Mai Watabe, Yuta Amagai, Young-Ho Lee, Shuji Akiyama and Kenji Inaba :
A unique leucine-valine adhesive motif supports structure and function of protein disulfide isomerase P5 via dimerization.,
Structure, Vol.29, No.12, 1357-1370.E6, 2021.

(要約): P5, also known as PDIA6, is a PDI family member involved in the ER quality control. Here, we revealed that P5 dimerizes via a unique adhesive motif contained in the N-terminal thioredoxin-like domain. Unlike conventional leucine zipper motifs with leucine residues every two helical turns on 30-residue parallel α helices, this adhesive motif includes periodic repeats of leucine/valine residues at the third or fourth position spanning five helical turns on 15-residue anti-parallel α helices. The P5 dimerization interface is further stabilized by several reciprocal salt bridges and C-capping interactions between protomers. A monomeric P5 mutant with the impaired adhesive motif showed structural instability and local unfolding, and behaved as aberrant proteins that induce the ER stress response. Disassembly of P5 to monomers compromised its ability to inactivate IRE1α via intermolecular disulfide bond reduction and its Ca-dependent regulation of chaperone function in vitro. Thus, the leucine-valine adhesive motif supports structure and function of P5.
(出版サイトへのリンク): ● Publication site (DOI): 10.1016/j.str.2021.03.016
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 33857433; ● Search Scopus @ Elsevier (PMID): 33857433; ● Search Scopus @ Elsevier (DOI): 10.1016/j.str.2021.03.016

(DOI: 10.1016/j.str.2021.03.016, PubMed: 33857433) Aya Okuda, Rintaro Inoue, Ken Morishima, Tomohide Saio, Yasuhiro Yunoki, Maho Yagi-Utsumi, Hirokazu Yagi, Masahiro Shimizu, Nobuhiro Sato, Reiko Urade, Koichi Kato and Masaaki Sugiyama :
Deuteration Aiming for Neutron Scattering.,
Biophysics and Physicobiology, Vol.18, 16-27, 2021.

(要約): The distinguished feature of neutron as a scattering probe is an isotope effect, especially the large difference in neutron scattering length between hydrogen and deuterium. The difference renders the different visibility between hydrogenated and deuterated proteins. Therefore, the combination of deuterated protein and neutron scattering enables the selective visualization of a target domain in the complex or a target protein in the multi-component system. Despite of this fascinating character, there exist several problems for the general use of this method: difficulty and high cost for protein deuteration, and control and determination of deuteration ratio of the sample. To resolve them, the protocol of protein deuteration techniques is presented in this report. It is strongly expected that this protocol will offer more opportunity for conducting the neutron scattering studies with deuterated proteins.
(出版サイトへのリンク): ● Publication site (DOI): 10.2142/biophysico.bppb-v18.003
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 33954079; ● Search Scopus @ Elsevier (PMID): 33954079; ● Search Scopus @ Elsevier (DOI): 10.2142/biophysico.bppb-v18.003

(DOI: 10.2142/biophysico.bppb-v18.003, PubMed: 33954079) Kamran Rizzolo, Hsiung Angela Yeou Yu, Adedeji Ologbenla, Rang Sa Kim, Haojie Zhu, Koichiro Ishimori, Guillaume Thibault, Elisa Leung, Wen Yi Zhang, Mona Teng, Marta Haniszewski, Noha Miah, Sadhna Phanse, Zoran Minic, Sukyeong Lee, Diaz Julio Caballero, Mohan Babu, F Francis T Tsai, Tomohide Saio and A Walid Houry :
Functional cooperativity between the trigger factor chaperone and the ClpXP proteolytic complex.,
Nature Communications, Vol.12, No.1, 2021.

(要約): A functional association is uncovered between the ribosome-associated trigger factor (TF) chaperone and the ClpXP degradation complex. Bioinformatic analyses demonstrate conservation of the close proximity of tig, the gene coding for TF, and genes coding for ClpXP, suggesting a functional interaction. The effect of TF on ClpXP-dependent degradation varies based on the nature of substrate. While degradation of some substrates are slowed down or are unaffected by TF, surprisingly, TF increases the degradation rate of a third class of substrates. These include λ phage replication protein λO, master regulator of stationary phase RpoS, and SsrA-tagged proteins. Globally, TF acts to enhance the degradation of about 2% of newly synthesized proteins. TF is found to interact through multiple sites with ClpX in a highly dynamic fashion to promote protein degradation. This chaperone-protease cooperation constitutes a unique and likely ancestral aspect of cellular protein homeostasis in which TF acts as an adaptor for ClpXP.
(キーワード): Binding Sites / Endopeptidase Clp / Escherichia coli / Escherichia coli Proteins / Gene Deletion / Genome, Bacterial / Magnetic Resonance Spectroscopy / Models, Biological / Models, Molecular / Molecular Chaperones / Mutagenesis / Peptides / Peptidylprolyl Isomerase / Phylogeny / Protein Binding / Protein Domains / Protein Interaction Mapping / Protein Multimerization / Proteolysis / Ribosomes / Substrate Specificity / Viral Proteins
(徳島大学機関リポジトリ): ● Metadata: 116608
(出版サイトへのリンク): ● Publication site (DOI): 10.1038/s41467-020-20553-x
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 33436616; ● Search Scopus @ Elsevier (PMID): 33436616; ● Search Scopus @ Elsevier (DOI): 10.1038/s41467-020-20553-x

(徳島大学機関リポジトリ: 116608, DOI: 10.1038/s41467-020-20553-x, PubMed: 33436616) Rintaro Inoue, Takashi Oda, Hiroshi Nakagawa, Taiki Tominaga, Tomohide Saio, Yukinobu Kawakita, Masahiro Shimizu, Aya Okuda, Ken Morishima, Nobuhiro Sato, Reiko Urade, Mamoru Sato and Masaaki Sugiyama :
Dynamics of proteins with different molecular structures under solution condition.,
Scientific Reports, Vol.10, No.1, 2020.

(要約): Incoherent quasielastic neutron scattering (iQENS) is a fascinating technique for investigating the internal dynamics of protein. However, low flux of neutron beam, low signal to noise ratio of QENS spectrometers and unavailability of well-established analyzing method have been obstacles for studying internal dynamics under physiological condition (in solution). The recent progress of neutron source and spectrometer provide the fine iQENS profile with high statistics and as well the progress of computational technique enable us to quantitatively reveal the internal dynamic from the obtained iQENS profile. The internal dynamics of two proteins, globular domain protein (GDP) and intrinsically disordered protein (IDP) in solution, were measured with the state-of-the art QENS spectrometer and then revealed with the newly developed analyzing method. It was clarified that the average relaxation rate of IDP was larger than that of GDP and the fraction of mobile H atoms of IDP was also much higher than that of GDP. Combined with the structural analysis and the calculation of solvent accessible surface area of amino acid residue, it was concluded that the internal dynamics were related to the highly solvent exposed amino acid residues depending upon protein's structure.
(キーワード): Amino Acids / Intrinsically Disordered Proteins / Molecular Dynamics Simulation / Molecular Structure / Protein Domains / Protein Folding / Protein Structure, Tertiary / Solutions / Solvents / Spectrum Analysis
(徳島大学機関リポジトリ): ● Metadata: 116638
(出版サイトへのリンク): ● Publication site (DOI): 10.1038/s41598-020-78311-4
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 33303822; ● Search Scopus @ Elsevier (PMID): 33303822; ● Search Scopus @ Elsevier (DOI): 10.1038/s41598-020-78311-4

(徳島大学機関リポジトリ: 116638, DOI: 10.1038/s41598-020-78311-4, PubMed: 33303822) Yuya Taguchi, Tomohide Saio and Daisuke Kohda :
Distance Distribution between Two Iodine Atoms Derived from Small-Angle X-ray Scattering Interferometry for Analyzing a Conformational Ensemble of Heavy Atom-Labeled Small Molecules.,
The Journal of Physical Chemistry Letters, Vol.11, No.14, 5451-5456, 2020.

(要約): To obtain unbiased information about the dynamic conformational ensemble of a molecule in solution, one promising approach is small-angle X-ray scattering (SAXS). Conventionally, SAXS data are converted to a pair distribution function, which describes the distance distribution between all pairs of atoms within a molecule. If two strong X-ray scatterers are introduced and the background contributions from the other atoms are suppressed, then the distance distribution between the two scatterers provides spatial information about a flexible molecule. Gold nanocrystals can provide such information for distances of >50 Å. Here, we synthesized a chemical compound containing two iodine atoms attached to the ends of a flexible polyethylene glycol chain and used the relevant singly labeled and unlabeled compounds to suppress the background contribution. This is a feasibility demonstration to prove that the distance distribution in the range of 10-30 Å can be experimentally accessed by SAXS.
(出版サイトへのリンク): ● Publication site (DOI): 10.1021/acs.jpclett.0c01107
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 32558579; ● Search Scopus @ Elsevier (PMID): 32558579; ● Search Scopus @ Elsevier (DOI): 10.1021/acs.jpclett.0c01107

(DOI: 10.1021/acs.jpclett.0c01107, PubMed: 32558579) Masaki Okumura, Kentaro Noi, Shingo Kanemura, Misaki Kinoshita, Tomohide Saio, Yuichi Inoue, Takaaki Hikima, Shuji Akiyama, Teru Ogura and Kenji Inaba :
Dynamic assembly of protein disulfide isomerase in catalysis of oxidative folding.,
Nature Chemical Biology, Vol.15, No.5, 499-509, 2019.

(要約): Time-resolved direct observations of proteins in action provide essential mechanistic insights into biological processes. Here, we present mechanisms of action of protein disulfide isomerase (PDI)-the most versatile disulfide-introducing enzyme in the endoplasmic reticulum-during the catalysis of oxidative protein folding. Single-molecule analysis by high-speed atomic force microscopy revealed that oxidized PDI is in rapid equilibrium between open and closed conformations, whereas reduced PDI is maintained in the closed state. In the presence of unfolded substrates, oxidized PDI, but not reduced PDI, assembles to form a face-to-face dimer, creating a central hydrophobic cavity with multiple redox-active sites, where substrates are likely accommodated to undergo accelerated oxidative folding. Such PDI dimers are diverse in shape and have different lifetimes depending on substrates. To effectively guide proper oxidative protein folding, PDI regulates conformational dynamics and oligomeric states in accordance with its own redox state and the configurations or folding states of substrates.
(キーワード): Biocatalysis / 小胞体 (endoplasmic reticulum) / Humans / Mutation / 酸化と還元 (oxidation and reduction) / Protein Conformation / Protein Disulfide-Isomerases / Protein Folding / Substrate Specificity
(出版サイトへのリンク): ● Publication site (DOI): 10.1038/s41589-019-0268-8
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 30992562; ● Search Scopus @ Elsevier (PMID): 30992562; ● Search Scopus @ Elsevier (DOI): 10.1038/s41589-019-0268-8

(DOI: 10.1038/s41589-019-0268-8, PubMed: 30992562) Soichiro Kawagoe, Hiroshi Nakagawa, Hiroyuki Kumeta, Koichiro Ishimori and Tomohide Saio :
Structural insight into proline cis/ trans isomerization of unfolded proteins catalyzed by the trigger factor chaperone,
The Journal of Biological Chemistry, Vol.293, No.39, 15095-15106, 2018.

(要約): Molecular chaperones often possess functional modules that are specialized in assisting the formation of specific structural elements, such as a disulfide bridges and peptidyl-prolyl bonds in cis form, in the client protein. A ribosome-associated molecular chaperone trigger factor (TF), which has a peptidyl-prolyl cis/trans isomerase (PPIase) domain, acts as a highly efficient catalyst in the folding process limited by peptidyl-prolyl isomerization. Herein we report a study on the mechanism through which TF recognizes the proline residue in the unfolded client protein during the cis/trans isomerization process. The solution structure of TF in complex with the client protein showed that TF recognizes the proline-aromatic motif located in the hydrophobic stretch of the unfolded client protein through its conserved hydrophobic cleft, which suggests that TF preferentially accelerates the isomerization of the peptidyl-prolyl bond that is eventually folded into the core of the protein in its native fold. Molecular dynamics simulation revealed that TF exploits the backbone amide group of Ile195 to form an intermolecular hydrogen bond with the carbonyl oxygen of the amino acid residue preceding the proline residue at the transition state, which presumably stabilizes the transition state and thus accelerates the isomerization. The importance of such intermolecular hydrogen-bond formation during the catalysis was further corroborated by the activity assay and NMR relaxation analysis.
(キーワード): Protein Conformation
(出版サイトへのリンク): ● Publication site (DOI): 10.1074/jbc.RA118.003579
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 30093407; ● Search Scopus @ Elsevier (PMID): 30093407; ● Search Scopus @ Elsevier (DOI): 10.1074/jbc.RA118.003579

(DOI: 10.1074/jbc.RA118.003579, PubMed: 30093407) Tomohide Saio, Soichiro Kawagoe, Koichiro Ishimori and G Charalampos Kalodimos :
Oligomerization of a molecular chaperone modulates its activity.,
eLife, Vol.7, e35731, 2018.

(要約): Molecular chaperones alter the folding properties of cellular proteins via mechanisms that are not well understood. Here, we show that Trigger Factor (TF), an ATP-independent chaperone, exerts strikingly contrasting effects on the folding of non-native proteins as it transitions between a monomeric and a dimeric state. We used NMR spectroscopy to determine the atomic resolution structure of the 100 kDa dimeric TF. The structural data show that some of the substrate-binding sites are buried in the dimeric interface, explaining the lower affinity for protein substrates of the dimeric compared to the monomeric TF. Surprisingly, the dimeric TF associates faster with proteins and it exhibits stronger anti-aggregation and holdase activity than the monomeric TF. The structural data show that the dimer assembles in a way that substrate-binding sites in the two subunits form a large contiguous surface inside a cavity, thus accounting for the observed accelerated association with unfolded proteins. Our results demonstrate how the activity of a chaperone can be modulated to provide distinct functional outcomes in the cell.
(キーワード): Binding Sites / 大腸菌 (Escherichia coli) / Escherichia coli Proteins / Molecular Chaperones / Peptidylprolyl Isomerase / Protein Binding / Protein Conformation / Protein Folding / Protein Multimerization
(出版サイトへのリンク): ● Publication site (DOI): 10.7554/eLife.35731
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 29714686; ● Summary page in Scopus @ Elsevier: 2-s2.0-85051931685

(DOI: 10.7554/eLife.35731, PubMed: 29714686, Elsevier: Scopus) Wataru Sato, Takeshi Uchida, Tomohide Saio and Koichiro Ishimori :
Polyethylene glycol promotes autoxidation of cytochrome c.,
Biochimica et Biophysica Acta (BBA) - General Subjects, Vol.1862, No.6, 1339-1349, 2018.

(要約): Cytochrome c (Cyt c) was rapidly oxidized by molecular oxygen in the presence, but not absence of PEG. The redox potential of heme c was determined by the potentiometric titration to be +236 ± 3 mV in the absence of PEG, which was negatively shifted to +200 ± 4 mV in the presence of PEG. The underlying the rapid oxidation was explored by examining the structural changes in Cyt c in the presence of PEG using UV-visible absorption, circular dichroism, resonance Raman, and fluorescence spectroscopies. These spectroscopic analyses suggested that heme oxidation was induced by a modest tertiary structural change accompanied by a slight shift in the heme position (<1.0 Å) rather than by partial denaturation, as is observed in the presence of cardiolipin. The near-infrared spectra showed that PEG induced dehydration from Cyt c, which triggered heme displacement. The primary dehydration site was estimated to be around surface-exposed hydrophobic residues near the heme center: Ile81 and Val83. These findings and our previous studies, which showed that hydrated water molecules around Ile81 and Val83 are expelled when Cyt c forms a complex with CcO, proposed that dehydration of these residues is functionally significant to electron transfer from Cyt c to CcO.
(キーワード): Cytochromes c / Electron Transport / Heme / Humans / 酸化と還元 (oxidation and reduction) / Oxygen / Polyethylene Glycols / Protein Conformation
(出版サイトへのリンク): ● Publication site (DOI): 10.1016/j.bbagen.2018.03.010
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 29540304; ● Search Scopus @ Elsevier (PMID): 29540304; ● Search Scopus @ Elsevier (DOI): 10.1016/j.bbagen.2018.03.010

(DOI: 10.1016/j.bbagen.2018.03.010, PubMed: 29540304)

MISC

Takahiro Muraoka, Tomohide Saio and Masaki Okumura :
Biophysical elucidation of neural network and chemical regeneration of neural tissue.,
Biophysics and Physicobiology, Vol.19, 2022.

(徳島大学機関リポジトリ): ● Metadata: 118277
(出版サイトへのリンク): ● Publication site (DOI): 10.2142/biophysico.bppb-v19.0024
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 36071879; ● Search Scopus @ Elsevier (PMID): 36071879; ● Search Scopus @ Elsevier (DOI): 10.2142/biophysico.bppb-v19.0024

(徳島大学機関リポジトリ: 118277, DOI: 10.2142/biophysico.bppb-v19.0024, PubMed: 36071879)

総説・解説

Soichiro Kawagoe, Koichiro Ishimori and Tomohide Saio :
Structural and Kinetic Views of Molecular Chaperones in Multidomain Protein Folding.,
International Journal of Molecular Sciences, Vol.23, No.5, Feb. 2022.

(要約): Despite recent developments in protein structure prediction, the process of the structure formation, folding, remains poorly understood. Notably, folding of multidomain proteins, which involves multiple steps of segmental folding, is one of the biggest questions in protein science. Multidomain protein folding often requires the assistance of molecular chaperones. Molecular chaperones promote or delay the folding of the client protein, but the detailed mechanisms are still unclear. This review summarizes the findings of biophysical and structural studies on the mechanism of multidomain protein folding mediated by molecular chaperones and explains how molecular chaperones recognize the client proteins and alter their folding properties. Furthermore, we introduce several recent studies that describe the concept of kinetics-activity relationships to explain the mechanism of functional diversity of molecular chaperones.
(キーワード): Humans / Kinetics / Molecular Chaperones / Protein Folding
(徳島大学機関リポジトリ): ● Metadata: 118276
(出版サイトへのリンク): ● Publication site (DOI): 10.3390/ijms23052485
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 35269628; ● Summary page in Scopus @ Elsevier: 2-s2.0-85125038979

(徳島大学機関リポジトリ: 118276, DOI: 10.3390/ijms23052485, PubMed: 35269628, Elsevier: Scopus) 川越聡一郎, Mori Eiichiro, 齋尾智英 :
分子シャペロンによる液–液相分離制御,
Thermal Medicine, Vol.37, No.2, 31-44, 2021年8月.

(出版サイトへのリンク): ● Publication site (DOI): 10.3191/thermalmed.37.31
(文献検索サイトへのリンク): ● CiNii @ 国立情報学研究所 (CRID): 1390570408616681984; ● Search Scopus @ Elsevier (DOI): 10.3191/thermalmed.37.31

(DOI: 10.3191/thermalmed.37.31, CiNii: 1390570408616681984) Takuya Yoshizawa, Ryu-Suke Nozawa, Z Tony Jia, Tomohide Saio and Eiichiro Mori :
Biological phase separation: cell biology meets biophysics.,
Biophysical Reviews, Vol.12, No.2, 519-539, Mar. 2020.

(要約): Progress in development of biophysical analytic approaches has recently crossed paths with macromolecule condensates in cells. These cell condensates, typically termed liquid-like droplets, are formed by liquid-liquid phase separation (LLPS). More and more cell biologists now recognize that many of the membrane-less organelles observed in cells are formed by LLPS caused by interactions between proteins and nucleic acids. However, the detailed biophysical processes within the cell that lead to these assemblies remain largely unexplored. In this review, we evaluate recent discoveries related to biological phase separation including stress granule formation, chromatin regulation, and processes in the origin and evolution of life. We also discuss the potential issues and technical advancements required to properly study biological phase separation.
(出版サイトへのリンク): ● Publication site (DOI): 10.1007/s12551-020-00680-x
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 32189162; ● Search Scopus @ Elsevier (PMID): 32189162; ● Search Scopus @ Elsevier (DOI): 10.1007/s12551-020-00680-x

(DOI: 10.1007/s12551-020-00680-x, PubMed: 32189162) 杉山正明, 井上倫太郎, 中川洋, 齋尾智英 :
中性子溶液散乱 -現在・過去・未来-,
波紋, Vol.30, No.1, 16-25, 2020年.

(要約): <p>Neutron has distinct features as a scattering probe to analyze structure and dynamics of biological macromolecules. The theme of this review is to try to describe how we did/do utilize them. And "How we should utilize them more effectively in the trend of integrative structural biology?" with solution scattering.</p>
(出版サイトへのリンク): ● Publication site (DOI): 10.5611/hamon.30.1_16
(文献検索サイトへのリンク): ● CiNii @ 国立情報学研究所 (CRID): 1390851165527349120; ● Search Scopus @ Elsevier (DOI): 10.5611/hamon.30.1_16

(DOI: 10.5611/hamon.30.1_16, CiNii: 1390851165527349120) 小田隆, 齋尾智英 :
検出技術 : 天然変性タンパク質の構造生物学 (特集相分離生物学 : 相分離メガネのススメ),
生物工学会誌, Vol.98, No.5, 232-235, 2020年.

(文献検索サイトへのリンク): ● CiNii @ 国立情報学研究所 (CRID): 1520853833284793216

(CiNii: 1520853833284793216) Tomohide Saio and Koichiro Ishimori :
Accelerating structural life science by paramagnetic lanthanide probe methods.,
Biochimica et Biophysica Acta (BBA) - General Subjects, Vol.1864, No.2, 129332, Mar. 2019.

(要約): We describe the recent progress of structural analysis methods exploiting paramagnetic lanthanide ions. In NMR spectroscopy, the paramagnetic effects induced by the trivalent lanthanide ions provide long-range (~40 Å) distance and angular information that can be exploited in protein structure determination, ligand screening, structure-based resonance assignment, and in-cell observation. The paramagnetic lanthanide ions can also be utilized in EPR spectroscopy, providing nanometer-scale distance measurement. These applications of the paramagnetic lanthanide probe are becoming more widespread by the use of a variety of lanthanide binding tags. Here, we introduce the basics of paramagnetic effects, several examples of lanthanide tags, and recent applications of paramagnetic lanthanide ions in NMR and EPR spectroscopy. Collectively, we show how the paramagnetic lanthanide probe accelerates research in protein science and drug design, and consequently life science.
(キーワード): Cysteine / Edetic Acid / Electron Spin Resonance Spectroscopy / Escherichia coli / Lanthanoid Series Elements / Ligands / Models, Molecular / Nuclear Magnetic Resonance, Biomolecular / Peptides / Protein Binding / Protein Conformation / Proteins
(出版サイトへのリンク): ● Publication site (DOI): 10.1016/j.bbagen.2019.03.018
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 30928492; ● Search Scopus @ Elsevier (PMID): 30928492; ● Search Scopus @ Elsevier (DOI): 10.1016/j.bbagen.2019.03.018

(DOI: 10.1016/j.bbagen.2019.03.018, PubMed: 30928492)

講演・発表

Tomohide Saio :
Depicting chaperone-mediated protein folding at residue-resolution,
International Symposium on Multifaceted Protein Dynamics, Fukuoka, Sep. 2024. Tomohide Saio :
Mechanistic insight into concerted action of a chaperone complex.,
The 8th International Symposium on Drug Discovery and Design by NMR, Yokohama, Aug. 2024. 齋尾智英 :
Visualizing conformational changes of a multidomain protein enzyme using paramagnetic probes,
International Society of Magnetic Resonance (ISMAR) 2023, ブリスベン, 2024年8月. Munehiro Kumashiro, Welegedara Adarshi, Otting Gottfried and Tomohide Saio :
Real-Time, Site-Specific Observation of Chaperone-Mediated Protein Folding using Noncanonical Amino Acid Labeling,
International Union for Pure and Applied Biophysics (IUPAB) 2024, Kyoto, Jun. 2024. Tomohide Saio :
Mechanistic insight into concerted action of a chaperone complex,
The 7th bilateralTaiwan-Japan NMR Symposium, Higashihiroshima, Feb. 2024. Tomohide Saio :
Integrative Structural Study on a Multidomain Protein Enzyme Utilizing Paramagnetic Lanthanide Ion,
Asia-Pacific Nuclear Magnetic Resonance (APNMR) 2023, Taipei, Sep. 2023. Tomohide Saio :
Conformational distribution of a multi-domain protein enzyme investigated by paramagnetic NMR and ESR,
3rd India-Japan NMR WORK SHOP, Online, Feb. 2023. Tomohide Saio :
NMR investigation of the regulators in protein folding and assembly,
ZOOMinar on Molecular Bases of Proteinopathies, Online, Feb. 2023. Tomohide Saio :
Structural and kinetic views of regulators for protein folding and assembly,
International Symposium: Protein Folding, Aggregation, Misfolding Disease, and Disease Crosstalk, Online, Sep. 2022. Tomohide Saio :
Conformational Variation of a Multi-Domain Protein Enzyme Investigated by Paramagnetic Lanthanide Probe,
ISMAR-APNMR2021, Aug. 2021. Tomohide Saio, Hiroshi Nakagawa, Soya Hiramatsu, Mizue Asada, Honoka Kawamukai, Toshikazu Nakamura and Koichiro Ishimori :
Application of a lanthanide tag for evaluation of conformational states of a multidomain protein,
IUCr 2021 - XXV General Assembly and Congress of the International Union of Crystallography, Aug. 2021. Tomohide Saio :
Mechanistic insights into a molecular chaperone in protein folding and degradation,
2021 virtual Cold Spring Harbor Asia Conference, Mar. 2021. Tomohide Saio :
NMR investigation of molecular chaperones manipulating protein folding,
Pacifichem 2021, 2021. Tomohide Saio :
Structural and kinetic insights into a molecular chaperone for protein folding, translocation, and degradation,
Pacifichem 2021, 2021. Kawamukai Honoka, Ishimori Koichiro and Tomohide Saio :
ALS-associated factor PRn inhibit the function of KapB2,
The 16th International Symposium of the Institute Network for Biomedical Sciences & KEY FORUM 2021 International Symposium, 2021. Tomohide Saio :
Mechanistic insight into chaperone-mediated protein homeostasis,
The 16th International Symposium of the Institute Network for Biomedical Sciences & KEY FORUM 2021 International Symposium, 2021. Tomohide Saio :
On and off between molecular chaperones and clients: Appropriate distance and timing for protein folding,
21st Hokudai-RIES International Symposium, Dec. 2020. 金村進吾, 橋本里菜, 松﨑元紀, 馬渕拓哉, 渡部マイ, 齋尾智英, 高山和雄, 李映昊, 奥村正樹 :
細胞外酸化還元酵素によるウイルス感染抑制機構の解明,
第24回日本蛋白質科学会年会, 2024年6月. 渡部マイ, 金村進吾, 鈴木琴乃, 坂和範, 松﨑元紀, 稲葉謙次, 中林孝和, 李映昊, 齋尾智英, 奥村正樹 :
小胞体局在酵素の相分離制御に対する活性酸素種および活性窒素種の影響,
第24回日本蛋白質科学会年会, 2024年6月. 武井梓穂, 宇賀神魁, 川越聡一郎, 齋尾智英, 松田正, 前仲勝実, 姚閔, 尾瀬農之 :
乳がん特異的キナーゼとアダプター蛋白質が形成する分子集合と酵素活性の相関を検証する,
第24回日本蛋白質科学会年会, 2024年6月. 森圭太, 齋尾智英, 村岡貴博 :
金属配位性ジスルフィド化合物によるタンパク質凝集抑制と酸化的フォールディング促進,
第24回日本蛋白質科学会年会, 2024年6月. 熊代宗弘, 久米田博之, Welegedara Adarshi, Qianzhu Haocheng, Abdelkader Elwy, Huber Thomas, Otting Gottfried, 齋尾智英 :
時間分解分光計測で明かす分子シャペロンによるタンパク質フォールディング促進機構,
第24回日本蛋白質科学会年会, 2024年6月. 松﨑元紀, 齋尾智英 :
PAGEを基盤とした抗原抗体反応における会合状態分布の解析,
第24回日本蛋白質科学会年会, 2024年6月. 川越聡一郎, 久米田博之, 齋尾智英 :
Heat shock factor-1のストレス応答性液-液相分離の構造基盤,
第24回日本蛋白質科学会年会, 2024年6月. 熊代宗弘, 齋尾智英 :
Mechanism of Chaperone-Assisted Protein Folding: Insight from a Variety of Time-Resolved Biophysical Methods,
第15回日本生物物理学会中国四国支部大会, 2024年5月. 齋尾智英 :
動的タンパク質複合体の構造・キネティクスの理解,
日本薬学会第144年会, 2024年3月. 松﨑元紀, 横山武司, 次田篤史, 金村進吾, 田尻道子, 明石知子, 野井健太郎, 齋尾智英, 稲葉謙次, 奥村正樹 :
小胞体ストレスセンサーIRE1による活性酸素種の直接的感知と分子シャペロンによるその制御,
日本農芸化学会2024年度大会, 2024年3月. 鈴木洸希, 野尻涼矢, 齋尾智英, 村岡貴博 :
速度論の観点から理解するシャペロンによるフォールディング制御メカニズム,
日本化学会第104春季年会, 2024年3月. 齋尾智英 :
相分離シャペロンの機能阻害メカニズム,
第46回日本分子生物学会年会, 2023年12月. 川越聡一郎, 馬渕拓哉, 久米田博之, 松﨑元紀, 熊代宗弘, 石森浩一郎, 齋尾智英 :
ストレスセンサーの会合を制御する多様な相互作用の分子機構,
第61回日本生物物理学会年会, 2023年11月. 服部良一, 熊代宗弘, 高麗王, 姜泰成, 久米田博之, 松﨑元紀, 齋尾智英 :
神経変性疾患関連変異によるプロリン異性化酵素PPIAのダイナミクス変調,
第 62回 NMR討論会, 2023年11月. 朱浩傑, 川越聡一郎, 久米田博之, 石森浩一郎, 齋尾智英 :
タンパク質アンフォールディングを担うシャペロン複合体の構造解析,
第 62回 NMR討論会, 2023年11月. 齋尾智英 :
液-液相分離制御と神経変性疾患の動的構造基盤,
第96回日本生化学会大会, 2023年11月. 松﨑元紀, 横山武司, 次田篤史, 金村進吾, 田尻道子, 明石知子, 野井健太郎, 齋尾智英, 稲葉謙次, 奥村正樹 :
小胞体ストレスセンサーIRE1 によるストレス感知と越膜シグナル変換の分子機構,
第96回日本生化学会, 2023年11月. 松﨑元紀, 横山武司, 次田篤史, 金村進吾, 田尻道子, 明石知子, 野井健太郎, 齋尾智英, 稲葉謙次, 奥村正樹 :
小胞体ストレスセンサーIRE1の多量体形成ポテンシャルとストレス感知,
第23回日本蛋白質科学会年会, 2023年7月. Tomohide Saio, 川向ほの香, 加藤胡都菜, Motonori Matsusaki, 久米田博之 and 石森浩一郎 :
Pro-Argポリジペプチドの毒性発現メカニズムの解明,
第23回蛋白質科学会, Vol.-, No.-, -, Jul. 2023. 齋尾智英 :
多様な結合様式を介した環境応答性相分離と相転移,
第23回蛋白質科学会年会, Vol.-, No.-, -, 2023年7月. 川越聡一郎, 馬渕拓哉, 久米田博之, 熊代宗弘, 石森浩一郎, 齋尾智英 :
局所構造形成と連動したheat shock factor-1の会合状態変化,
第23回日本蛋白質科学会年会, 2023年7月. 齋尾智英 :
ランタノイドタグを用いた蛋白質の動的構造解析,
日本化学会第103春季年会(2023), 2023年3月. 齋尾智英 :
常磁性プローブを用いたマルチドメインタンパク質の構造解析,
蛋白研セミナー基礎から学ぶ最新NMR解析法第6回ワークショップ統合型構造生物学研究, 2023年3月. Tomohide Saio :
Structural insight into regulation and dysregulation of protein assembly and folding,
The 1st IMEG Meeting of The Research Center for High Depth Omics, Jan. 2023. 齋尾智英 :
シャペロンから解き明かすタンパク質フォールディングと集合の分子メカニズム,
第18回Organelle zone seminar, 2022年12月. 齋尾智英 :
相分離制御と制御破綻の分子メカニズム,
2022 年度日本分光学会NMR分光部会集中講義, 2022年10月. 齋尾智英 :
分子から理解する相分離制御と破綻,
第 74 回日本細胞生物学会年会, 2022年6月. 川越聡一郎, 松﨑元紀, 石森浩一郎, 齋尾智英 :
高次多量体形成が駆動するheat shock factor-1液滴の酸化的相転移,
第 22 回日本蛋白質科学会年会, 2022年6月. 川向ほの香, 石森浩一郎, 齋尾智英 :
核輸送因子Kapβ2のFUSに対する液-液相分離制御におけるPro-Argポリジペプチドによる阻害機構の解明,
第 22 回日本蛋白質科学会年会, 2022年6月. 齋尾智英 :
シャペロンにおけるキネティクス-活性相関,
第 22 回日本蛋白質科学会年会, 2022年6月. 齋尾智英 :
シャペロンによるタンパク質集合とフォールディングの制御機構,
千里ライフサイエンスセミナーV1 相分離がもたらす医療・創薬の新展開, 2022年5月. 齋尾智英 :
NMRを中核とした統合的解析でタンパク質の動きを捉える,
蛋白研フロンティアセミナー, 2022年4月. 齋尾智英 :
タンパク質液滴の形成・制御・破綻の分子メカニズム,
日本化学会第102春季年会, 2022年3月. 松﨑元紀, 横山武司, 次田篤史, 金村進吾, 田尻道子, 明石知子, 齋尾智英, 稲葉謙次, 奥村正樹 :
小胞体ストレスセンサーの会合状態分布を介した応答制御機構の研究,
日本農芸化学会2022年度大会, 2022年3月. 太田帆香, 川越聡一郎, 松﨑元紀, 久米田博之, 石森浩一郎, 齋尾智英 :
新規光応答性シャペロンの創製とそれを利用した液-液相分離の制御,
2021年度生物物理学会北海道支部-東北支部合同例会, 2022年3月. 岡田莉奈, 金村進吾, 黒井邦巧, 松﨑元紀, 齋尾智英, 山口宏, 伊藤大, 李映昊, 中林孝和, 稲葉謙次, 奥村正樹 :
酸化還元制御によるヒトガレクチン1の構造機能調節の理解(Understanding the role of redox-regulated galectin-1 function),
第44回日本分子生物学会年会, 2021年12月. 川越聡一郎, 松﨑元紀, 石森浩一郎, 齋尾智英 :
ストレス応答を制御する転写因子Heat shock factor1の酸化還元依存的な相転移,
第44回日本分子生物学会年会, 2021年12月. 齋尾智英 :
多量体形成を介したシャペロンの機能制御,
第44回日本分子生物学会年会, 2021年12月. 齋尾智英 :
速度論の観点から理解するシャペロンによるフォールディング制御メカニズム,
学術変革B「遅延制御超分子化学」キックオフシンポジウム, 2021年11月. Tomohide Saio :
Large-scale conformational distribution of a multi-domain protein enzyme investigated by NMR and EPR,
第59回日本生物物理学会年会, Nov. 2021. 齋尾智英 :
常磁性金属と分子シャペロン,
2020年度日本分光学会NMR分光部会集中講義, 2020年10月. Tomohide Saio and 石森浩一郎 :
Exploiting paramagnetic metal ions for protein structural study in solution,
The 58th Annual Meeting of the BSJ, Sep. 2020. 齋尾智英 :
シャペロンから理解する細胞内タンパク質の動態制御メカニズム,
第93回日本生化学会大会, 2020年9月.

研究会・報告書: 齋尾智英 :
シャペロンによるフォールディングと分子集合の制御メカニズム,
日本薬学会構造活性相関部会構造活性フォーラム2023, 2024年8月. 齋尾智英 :
生命を駆動する動的分子認識の理解,
徳島大学医光融合研究シンポジウム, 2024年3月. 齋尾智英 :
生命を駆動する動的相互作用の機序解明,
奈良県立医科大学 V-iCliniX講座最終成果報告会, 2024年2月. 齋尾智英 :
シャペロンから解き明かすタンパク質フォールディングと集合の制御メカニズム,
R022 量子構造生物学委員会第 11 回研究会, 2023年11月. 齋尾智英 :
生命を駆動する弱い相互作用の探究,
第18回オールスター最先端セミナー, 2023年11月. 齋尾智英 :
生体分子の弱い相互作用をNMRで可視化する,
東京大学「産学連携研究会」, 2023年9月. 齋尾智英 :
シャペロンによるフォールディングとタンパク質集合の制御メカニズム,
日本薬学会構造活性相関部会構造活性フォーラム2023, Vol.-, No.-, -, 2023年8月. Tomohide Saio :
NMR investigation of the regulators in protein folding and assembly,
International symposium on Kinetics-driven supramolecular chemistry, Vol.-, No.-, -, Jul. 2023. 齋尾智英 :
シャペロンによるタンパク質集合とフォールディングの制御機構,
千里ライフサイエンスセミナー, Vol.-, No.-, -, 2023年5月. 齋尾智英 :
NMRを中核とした統合的解析でタンパク質の動きを捉える,
蛋白研フロンティアセミナー, Vol.-, No.-, -, 2023年4月. 齋尾智英, 宮ノ入洋平, 中川敦史, 八木宏昌, 木川隆則, 矢吹孝, 松田夏子, 竹内恒, 小橋川敬博, 坂倉正義, 幸福裕 :
蛋白研セミナー基礎から学ぶ最新 NMR 解析法 – NMR試料の調製,
次世代NMRワーキンググループ, 2021年12月. 齋尾智英 :
シャペロンによる分子集合制御,
第5回LLPS研究会, 2021年9月.

特許: 奥村正樹, 稲葉謙次, 松﨑元紀, 金村進吾, 齋尾智英 : 液滴およびその製造方法, 特願2022-502960 (2021年6月), (2022年12月), 特許第7194403号.
作品: 研究者総覧に該当データはありませんでした。
補助金・競争的資金: 植物特化代謝マシナリの超分子解剖：膜アセンブル工学と多元構造解析による統合的理解 (研究課題/領域番号: 23H05470 )
パターン認識に基づくタンパク質集合状態の層別化が拓く相分離制御因子スクリーニング (研究課題/領域番号: 23K26688 )
光技術と構造生物学の融合による過渡構造解析 (研究課題/領域番号: 22K18361 )
プロミスカス認識の集積によるシャペロンの機能調節メカニズム (研究課題/領域番号: 23K23824 )
生体分子の構造形成における遅延制御メカニズム解明 (研究課題/領域番号: 21H05094 )
遅延制御超分子化学の推進 (研究課題/領域番号: 21H05093 )
小胞体シャペロンによるフォールディング中間体の過渡的認識と制御の構造基盤 (研究課題/領域番号: 20KK0156 )
生物学的相分離の制御機構 (研究課題/領域番号: 20H03199 )
相分離を介したシグナル伝達制御の構造基盤 (研究課題/領域番号: 19H04945 )
半特異的認識を介したシャペロンネットワークの構造基盤 (研究課題/領域番号: 19K06504 )
新世代中性子構造生物学の開拓 (研究課題/領域番号: 18H05229 )
NMRを主体としたタンパク質構造推移解析のための複合手法の開発と応用 (研究課題/領域番号: 17H05867 )
分子シャペロンの基質選択と活性発現における動的構造基盤 (研究課題/領域番号: 17H05657 )
ミトコンドリア呼吸鎖における電子伝達複合体の動的構造解析と電子伝達制御機構の解明 (研究課題/領域番号: 16H04173 )
NMRを主体としたタンパク質構造推移解析のための複合手法の開発と応用 (研究課題/領域番号: 15H01624 )
常磁性プローブを用いた呼吸鎖における電子伝達機構の解析 (研究課題/領域番号: 15K20829 )
ナノディスクを利用したミトコンドリア呼吸鎖における電子伝達機構の解析 (研究課題/領域番号: 25288072 )
研究者番号（80740802）による検索

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2024年11月15日更新

専門分野・研究分野: 生物物理学 (Biophysics)
所属学会・所属協会: ISMAR-APNMR2021
The Journal of the Korean Magnetic Resonance Society
ASUKA若手交流会
日本核磁気共鳴学会
日本生物物理学会
日本蛋白質科学会
第63回NMR討論会
第32回日本Cell Death学会学術集会
日本生化学会
2024 Joint Conference - Korean Society for Protein Science & Protein Science Society of Japan
2025 Joint Conference - Korean Society for Protein Science & Protein Science Society of Japan
委員歴・役員歴: ISMAR-APNMR2021 (プログラム委員 [2019年2月〜2021年8月])
The Journal of the Korean Magnetic Resonance Society (Editorial Board [2018年9月〜9999年])
ASUKA若手交流会 (プログラム委員 [2019年7月〜9999年])
日本核磁気共鳴学会 (評議員 [2021年4月〜2023年3月])
日本核磁気共鳴学会 (評議委員 [2021年4月〜2025年3月])
日本核磁気共鳴学会 (日本核磁気共鳴学会機関誌編集委員 [2022年4月〜2026年3月])
日本生物物理学会 (2022年分野別専門委員 [2022年1月〜12月])
日本蛋白質科学会 (執行役員 [2023年4月〜2025年3月])
第63回NMR討論会 (プログラム委員 [2023年〜2024年11月])
第32回日本Cell Death学会学術集会 (プログラム委員 [2023年11月〜2024年7月])
日本生化学会 (評議員 [2024年4月〜2026年3月])
日本生物物理学会 (代議員 [2023年4月〜2027年3月])
2024 Joint Conference - Korean Society for Protein Science (KSPS) & Protein Science Society of Japan (PSSJ) (実行委員 [2024年2月〜6月])
2025 Joint Conference - Korean Society for Protein Science (KSPS) & Protein Science Society of Japan (PSSJ) (実行委員 [2024年8月〜2025年6月])
受賞: 2021年3月, ALS研究助成基金 (公益信託「生命の彩」)
2021年7月, 2021年度研究助成 (公益財団法人武田化学振興財団)
2021年7月, 2021年度研究助成 (公益信託加藤記念難病研究助成基金)
2021年10月, 最優秀理事長賞 (公益財団法人アステラス病態代謝研究会)
2022年9月, 徳島大学学⻑表彰 (徳島大学)
2023年9月, 徳島大学学⻑表彰 (徳島大学)
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Ｊグローバル

Jグローバル最終確認日: 2024/11/9 01:14
氏名（漢字）: 齋尾智英
氏名（フリガナ）: サイオトモヒデ
氏名（英字）: Saio Tomohide
所属機関: 徳島大学教授

リサーチマップ

researchmap最終確認日: 2024/11/10 03:41
氏名（漢字）: 齋尾智英
氏名（フリガナ）: サイオトモヒデ
氏名（英字）: Saio Tomohide
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登録日時: 2015/6/16 14:01
更新日時: 2024/11/4 15:26
アバター画像URI: https://researchmap.jp/tsaio/avatar.jpg
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所属ID: 0344000000
所属: 徳島大学
部署: 先端酵素学研究所
職名: 教授
学位: 博士(生命科学)
学位授与機関: 北海道大学
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研究者番号: 80740802

所属（現在）: 2024/4/1 : 徳島大学, 先端酵素学研究所, 教授

所属（過去の研究課題 情報に基づく）*注記: 2020/4/1 – 2024/4/1 : 徳島大学, 先端酵素学研究所, 教授
2016/4/1 – 2020/4/1 : 北海道大学, 理学研究院, 助教
2015/4/1 : 北海道大学, 理学(系)研究科(研究院), 助教
2015/4/1 : 北海道大学, 大学院理学研究院, 助教

審査区分/研究分野

研究代表者

生物系 / 生物学 / 生物科学 / 構造生物化学 / 生物系 / 生物学 / 生物科学 / 分子生物学
小区分43020:構造生物化学関連
生物系
中区分43:分子レベルから細胞レベルの生物学およびその関連分野
複合領域
学術変革領域研究区分(Ⅱ)

研究代表者以外

理工系 / 化学 / 複合化学 / 生体関連化学
大区分B
小区分43020:構造生物化学関連
学術変革領域研究区分(Ⅱ)
中区分38:農芸化学およびその関連分野
大区分F
小区分34020:分析化学関連

キーワード

研究代表者

呼吸鎖 / 電子伝達 / NMR / 立体構造 / ダイナミクス / 常磁性ランタニド / 溶液構造 / シャペロン複合体 / 立体構造解析 / 常磁性金属 / シャペロン / 複合体立体構造 / 過渡的相互作用 / 分子シャペロン / 結合解離速度 / フォールディング / プロリン異性化 / 高速AFM / 速度論 / 二量体 / トリガーファクター / タンパク質フォールディング / 小胞体 / フォールディング中間体 / 常磁性タグ / MurD / ランタニドイオン / 常磁性 / 核磁気共鳴法 / マルチドメインタンパク質 / 細胞壁合成 / 構造変化 / 活性制御 / 常磁性ランタノイドイオン / ESR / SAXS / ランタノイド / 遅延制御 / キネティクス / 蛋白質フォールディング / 結合キネティクス / 光技術 / 中性子散乱 / 過渡的構造 / 液-液相分離 / LCタンパク質 / 天然変性タンパク質 / 相分離シャペロン / 相互作用解析 / 多量体

研究代表者以外

シトクロムc酸化酵素 / シトクロムc / ナノディスク / 電子伝達反応 / ヘム / MSP / ドッキングシミュレーション / 構造揺らぎ / 生体膜モデル / シトクロム酸化酵素 / 電子伝達系 / ミトコンドリア呼吸鎖 / 電子伝達 / TCS / 電子伝達経路 / 脱水和 / 構造的揺らぎ / 電子伝達複合体 / 中性子散乱 / 生体高分子ダイナミクス / 重水素化 / 分子動力学シミュレーション / 階層間連携ダイナミクス / 中性子溶液散乱 / タンパク質重水素化 / ドメインライゲーション / 計算機連携解析 / 新世代中性子構造生物学 / ドメイン選択重水素化 / 分子動力学計算 / 階層関連ダイナミクス / 蛋白質重水素化 / 蛋白質階層間連携ダイナミクス / MD連携解析 / 中性子準弾性散乱 / 租視化分子動力学計算 / 蛋白質ダイナミクス / LCドメイン / cross-βポリマー / 生物学的相分離 / アミロイド様線維 / 相分離シャペロン / 相分離駆動 / 相分離制御 / 相分離破綻 / 相分離生物学 / 天然変性タンパク質 / 中間径フィラメント / アミロイド線維 / 液-液相分離 / LLPS / 低複雑性配列 / cross-β polymer / 遅延制御 / 超分子化学 / タンパク質 / フォールディング / ミスフォールディング / 植物特化代謝 / メタボロン / タンパク質間相互作用 / フラボノイド / 天然ゴム / 相互作用 / パターン認識 / 蛍光プローブ / 神経変性疾患

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齋尾 智英

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研究代表者

研究代表者以外

研究代表者

研究代表者以外

齋尾智英