徳島大学 / 教育研究者総覧 --- 松﨑元紀

個人のホームページ

https://researchmap.jp/matsusaki_motonori (researchmap)

https://orcid.org/0000-0002-7296-033X (ORCID)

専門分野

○	ライフサイエンス (Life sciences) [分子生物学 (Molecular biology)]
○	ライフサイエンス (Life sciences) [食品科学 (Food sciences)]

研究テーマ

著書・論文

(著書・論文等の業績についてはhttps://researchmap.jp/matsusaki_motonori (researchmap)でも御覧頂けます．)

学術論文(審査論文):

1.	ALi Hanif, YAMANISHI Mone, TSUCHIYA Miki, Hasi Yesmin Rumana, Motonori Matsusaki, Tomohide Saio, Mutsumi Aihara, Ryushi Kawakami and Tamotsu Tanaka : Solubilization of saturated fatty acids and its lysophosphatidylcholine by complexation with bovine serum albumin, Lipids, 2025. (要約) High plasma levels of saturated fatty acids (SFAs) are associated with lifestyle diseases such as atherosclerosis and diabetes, whereas the accumulation of very long-chain fatty acids (VLCFAs) is believed to be responsible for neuropathy in certain types of peroxisomal disorders. Despite their clinical relevance, the toxicity mechanisms of fatty acids (FAs) remain poorly understood, largely because of the challenges in solubilizing them for in vitro experiments. We recently developed a method to form stable complexes of FAs with bovine serum albumin (BSA) using isopropanol as the solvent. Here, we demonstrate the stability and concentration range of FA/BSA and lysophosphatidylcholine (LysoPtdCho)/BSA complexes prepared using this method. These complexes exhibit enhanced solubility, retain their biological activity in cellular uptake assays, and remain stable for up to 12 months. We believe that our method will contribute to a better understanding of the toxicity and metabolism of SFAs and SFA-LysoPtdChos, and offer new insights into their roles in metabolic diseases and peroxisomal disorders. (徳島大学機関リポジトリ) ● Metadata: 2013472 (出版サイトへのリンク) ● Publication site (DOI): 10.1002/lipd.70005 (文献検索サイトへのリンク) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 40937877 ● Search Scopus @ Elsevier (PMID): 40937877 ● Search Scopus @ Elsevier (DOI): 10.1002/lipd.70005 (徳島大学機関リポジトリ: 2013472, DOI: 10.1002/lipd.70005, PubMed: 40937877)
2.	Yoshikazu Hattori, Munehiro Kumashiro, Hiroyuki Kumeta, Taisei Kyo, Soichiro Kawagoe, Motonori Matsusaki and Tomohide Saio : A Disease-Associated Mutation Impedes PPIA through Allosteric Dynamics Modulation, Biochemistry, 64, 14, 2971-2975, 2025. (出版サイトへのリンク) ● Publication site (DOI): 10.1021/acs.biochem.5c00260 (文献検索サイトへのリンク) ● Summary page in Scopus @ Elsevier: 2-s2.0-105009433118 (DOI: 10.1021/acs.biochem.5c00260, Elsevier: Scopus)
3.	Soichiro Kawagoe, Motonori Matsusaki, Takuya Mabuchi, Yuto Ogasawara, Kazunori Watanabe, Koichiro Ishimori and Tomohide Saio : Mechanistic Insights Into Oxidative Response of Heat Shock Factor 1 Condensates, JACS Au, 5, 2, 606-617, 2025. (キーワード) biological phase transition / biophysics / heat shock factor 1 / oxidative hyper-oligomerization / stress response (出版サイトへのリンク) ● Publication site (DOI): 10.1021/jacsau.4c00578 (文献検索サイトへのリンク) ● Summary page in Scopus @ Elsevier: 2-s2.0-85216615817 (DOI: 10.1021/jacsau.4c00578, Elsevier: Scopus)
4.	Koki Suzuki, Ryoya Nojiri, Motonori Matsusaki, Takuya Mabuchi, Shingo Kanemura, Kotone Ishii, Hiroyuki Kumeta, Masaki Okumura, Tomohide Saio and Takahiro Muraoka : Redox-active chemical chaperones exhibiting promiscuous binding promote oxidative protein folding under condensed sub-millimolar conditions, Chemical Science, 15, 32, 12676-12685, 2024. (出版サイトへのリンク) ● Publication site (DOI): 10.1039/d4sc02123a (文献検索サイトへのリンク) ● Summary page in Scopus @ Elsevier: 2-s2.0-85199765159 (DOI: 10.1039/d4sc02123a, Elsevier: Scopus)
5.	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, 10, 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: 2009344 (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): 1050867133849684096 ● Summary page in Scopus @ Elsevier: 2-s2.0-85118999409 (徳島大学機関リポジトリ: 2009344, DOI: 10.3390/biology10111112, CiNii: 1050867133849684096, Elsevier: Scopus)
6.	Haojie Zhu, Motonori Matsusaki, Taiga Sugawara, Koichiro Ishimori and Tomohide Saio : Zinc-Dependent Oligomerization of Thermus thermophilus Trigger Factor Chaperone, Biology, 10, 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: 2010008 (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: 2010008, DOI: 10.3390/biology10111106, PubMed: 34827099)
7.	Yuya Tanikawa, Shingo Kanemura, Dai Ito, Yuxi Lin, Motonori Matsusaki, Kimiko Kuroki, Hiroshi Yamaguchi, Katsumi Maenaka, Young-Ho Lee, Kenji Inaba and Masaki Okumura : Ca Regulates ERp57-Calnexin Complex Formation., Molecules, 26, 10, 2853, 2021. (要約) ERp57, a member of the protein disulfide isomerase family, is a ubiquitous disulfide catalyst that functions in the oxidative folding of various clients in the mammalian endoplasmic reticulum (ER). In concert with ER lectin-like chaperones calnexin and calreticulin (CNX/CRT), ERp57 functions in virtually all folding stages from co-translation to post-translation, and thus plays a critical role in maintaining protein homeostasis, with direct implication for pathology. Here, we present mechanisms by which Ca regulates the formation of the ERp57-calnexin complex. Biochemical and isothermal titration calorimetry analyses revealed that ERp57 strongly interacts with CNX via a non-covalent bond in the absence of Ca. The ERp57-CNX complex not only promoted the oxidative folding of human leukocyte antigen heavy chains, but also inhibited client aggregation. These results suggest that this complex performs both enzymatic and chaperoning functions under abnormal physiological conditions, such as Ca depletion, to effectively guide proper oxidative protein folding. The findings shed light on the molecular mechanisms underpinning crosstalk between the chaperone network and Ca. (キーワード) Calcium / Calnexin / Disulfides / Humans / Models, Biological / Oxidation-Reduction / Protein Aggregates / Protein Binding / Protein Disulfide-Isomerases / Protein Folding / Thermodynamics (徳島大学機関リポジトリ) ● Metadata: 2010085 (出版サイトへのリンク) ● Publication site (DOI): 10.3390/molecules26102853 (文献検索サイトへのリンク) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 34064874 ● Search Scopus @ Elsevier (PMID): 34064874 ● Search Scopus @ Elsevier (DOI): 10.3390/molecules26102853 (徳島大学機関リポジトリ: 2010085, DOI: 10.3390/molecules26102853, PubMed: 34064874)
8.	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, 29, 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)
9.	Shunsuke Okada, Motonori Matsusaki, Masaki Okumura and Takahiro Muraoka : Conjugate of Thiol and Guanidyl Units with Oligoethylene Glycol Linkage for Manipulation of Oxidative Protein Folding., Molecules, 26, 4, 879, 2021. (要約) Oxidative protein folding is a biological process to obtain a native conformation of a protein through disulfide-bond formation between cysteine residues. In a cell, disulfide-catalysts such as protein disulfide isomerase promote the oxidative protein folding. Inspired by the active sites of the disulfide-catalysts, synthetic redox-active thiol compounds have been developed, which have shown significant promotion of the folding processes. In our previous study, coupling effects of a thiol group and guanidyl unit on the folding promotion were reported. Herein, we investigated the influences of a spacer between the thiol group and guanidyl unit. A conjugate between thiol and guanidyl units with a diethylene glycol spacer (GdnDEG-SH) showed lower folding promotion effect compared to the thiol-guanidyl conjugate without the spacer (GdnSH). Lower acidity and a more reductive property of the thiol group of GdnDEG-SH compared to those of GdnSH likely resulted in the reduced efficiency of the folding promotion. Thus, the spacer between the thiol and guanidyl groups is critical for the promotion of oxidative protein folding. (キーワード) Catalysis / Cysteine / Disulfides / Ethylene Glycol / Glutathione / Kinetics / Oxidation-Reduction / Oxidative Stress / Protein Disulfide-Isomerases / Protein Folding / Sulfhydryl Compounds (出版サイトへのリンク) ● Publication site (DOI): 10.3390/molecules26040879 (文献検索サイトへのリンク) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 33562280 ● Search Scopus @ Elsevier (PMID): 33562280 ● Search Scopus @ Elsevier (DOI): 10.3390/molecules26040879 (DOI: 10.3390/molecules26040879, PubMed: 33562280)
10.	Shingo Kanemura, Motonori Matsusaki, Kenji Inaba and Masaki Okumura : PDI Family Members as Guides for Client Folding and Assembly., International Journal of Molecular Sciences, 21, 24, 9351, 2020. (要約) Complicated and sophisticated protein homeostasis (proteostasis) networks in the endoplasmic reticulum (ER), comprising disulfide catalysts, molecular chaperones, and their regulators, help to maintain cell viability. Newly synthesized proteins inserted into the ER need to fold and assemble into unique native structures to fulfill their physiological functions, and this is assisted by protein disulfide isomerase (PDI) family. Herein, we focus on recent advances in understanding the detailed mechanisms of PDI family members as guides for client folding and assembly to ensure the efficient production of secretory proteins. (キーワード) Animals / Calnexin / Calreticulin / Humans / Protein Disulfide-Isomerases / Protein Folding / Protein Multimerization / Proteostasis (出版サイトへのリンク) ● Publication site (DOI): 10.3390/ijms21249351 (文献検索サイトへのリンク) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 33302492 ● Search Scopus @ Elsevier (PMID): 33302492 ● Search Scopus @ Elsevier (DOI): 10.3390/ijms21249351 (DOI: 10.3390/ijms21249351, PubMed: 33302492)
11.	Aya Okuda, Motonori Matsusaki, Taro Masuda, Ken Morishima, Nobuhiro Sato, Rintaro Inoue, Masaaki Sugiyama and Reiko Urade : A novel soybean protein disulphide isomerase family protein possesses dithiol oxidation activity: identification and characterization of GmPDIL6., The Journal of Biochemistry, 168, 4, 393-405, 2020. (要約) Secretory and membrane proteins synthesized in the endoplasmic reticulum (ER) are folded with intramolecular disulphide bonds, viz. oxidative folding, catalysed by the protein disulphide isomerase (PDI) family proteins. Here, we identified a novel soybean PDI family protein, GmPDIL6. GmPDIL6 has a single thioredoxin-domain with a putative N-terminal signal peptide and an active centre (CKHC). Recombinant GmPDIL6 forms various oligomers binding iron. Oligomers with or without iron binding and monomers exhibited a dithiol oxidase activity level comparable to those of other soybean PDI family proteins. However, they displayed no disulphide reductase and extremely low oxidative refolding activity. Interestingly, GmPDIL6 was mainly expressed in the cotyledon during synthesis of seed storage proteins and GmPDIL6 mRNA was up-regulated under ER stress. GmPDIL6 may play a role in the formation of disulphide bonds in nascent proteins for oxidative folding in the ER. (キーワード) Amino Acid Sequence / Cloning, Molecular / Endoplasmic Reticulum / Oxidation-Reduction / Protein Disulfide-Isomerases / Protein Folding / Sequence Homology / Soybeans / Toluene (出版サイトへのリンク) ● Publication site (DOI): 10.1093/jb/mvaa058 (文献検索サイトへのリンク) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 32458972 ● Search Scopus @ Elsevier (PMID): 32458972 ● Search Scopus @ Elsevier (DOI): 10.1093/jb/mvaa058 (DOI: 10.1093/jb/mvaa058, PubMed: 32458972)
12.	Motonori Matsusaki, Shingo Kanemura, Misaki Kinoshita, Young-Ho Lee, Kenji Inaba and Masaki Okumura : The Protein Disulfide Isomerase Family: from proteostasis to pathogenesis., Biochimica et Biophysica Acta (BBA) - General Subjects, 1864, 2, 129338, 2019. (要約) In mammalian cells, nearly one-third of proteins are inserted into the endoplasmic reticulum (ER), where they undergo oxidative folding and chaperoning assisted by approximately 20 members of the protein disulfide isomerase family (PDIs). PDIs consist of multiple thioredoxin-like domains and recognize a wide variety of proteins via highly conserved interdomain flexibility. Although PDIs have been studied intensely for almost 50 years, exactly how they maintain protein homeostasis in the ER remains unknown, and is important not only for fundamental biological understanding but also for protein misfolding- and aggregation-related pathophysiology. Herein, we review recent advances in structural biology and biophysical approaches that explore the underlying mechanism by which PDIs fulfil their distinct functions to promote productive protein folding and scavenge misfolded proteins in the ER, the primary factory for efficient production of the secretome. (キーワード) Animals / Disulfides / Endoplasmic Reticulum / Humans / Membrane Glycoproteins / Mice / Mutation / Neurodegenerative Diseases / Oxidation-Reduction / Oxidative Stress / Peptides / Protein Denaturation / Protein Disulfide-Isomerases / Protein Domains / Protein Folding / Rats (出版サイトへのリンク) ● Publication site (DOI): 10.1016/j.bbagen.2019.04.003 (文献検索サイトへのリンク) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 30986509 ● Search Scopus @ Elsevier (PMID): 30986509 ● Search Scopus @ Elsevier (DOI): 10.1016/j.bbagen.2019.04.003 (DOI: 10.1016/j.bbagen.2019.04.003, PubMed: 30986509)

総説・解説:

1.	金村進吾, 松﨑元紀, 前仲勝実, 稲葉謙次, 奥村正樹 : 小胞体におけるMHCの品質管理 (特集 MHCバイオロジー), 臨床免疫·アレルギー科, 74, 5, 419-426, 2020年11月. (文献検索サイトへのリンク) ● CiNii @ 国立情報学研究所 (CRID): 1523669554901025920 (CiNii: 1523669554901025920)

国際会議:

1.	Motonori Matsusaki, Tomohide Saio, Inaba Kenji and Okumura Masaki : Higher-order Oligomerization of IRE1 Luminal Domain Modulates Unfolded Protein Response, 16th ER and Redox club meeting, Namur, Mar. 2025.
2.	Motonori Matsusaki and Tomohide Saio : High-resolution visualization of heterogenous protein assembly, Korea-Japan International Symposium on Protein Science (Joint Conference), Sapporo, Jun. 2024.

国内講演発表:

1.	服部良一, 熊代宗弘, 久米田博之, 姜泰成, 川越聡一郎, 松﨑元紀, 齋尾智英 : ALS関連変異によって引き起こされるPPIAダイナミクス変調, 第64回 NMR討論会, 2025年11月.
2.	高麗王, 服部良一, 松﨑元紀, 齋尾智英 : 分子シャペロンCypAによるALS関連タンパク質の相分離及びアミロイド線維形成制御, 第98回日本生化学会大会, 2025年11月.
3.	Tuan Thanh Do, Motonori Matsusaki, Soichiro Kawagoe, Kumeta Hiroyuki and Tomohide Saio : OptoChaperone-A Biohybrid Tool Regulating Protein Condensates in vitro and in Cells, 第63回日本生物物理学会年会, Sep. 2025.
4.	高麗王, 服部良一, 松﨑元紀, 齋尾智英 : シャペロンによるALS関連タンパク質の相分離制御機構, 第 25 回日本蛋白質科学会年会, 2025年6月.
5.	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 : 疾患関連変異によって引き起こされる酵素の動的アロステリック効果, 第 25 回日本蛋白質科学会年会, 2025年6月.
6.	渡部マイ, 金村進吾, 鈴木琴乃, 坂和範, 佐藤伸一, 松﨑元紀, 稲葉謙次, 中林考和, 李映昊, 齋尾智英, 奥村正樹 : タンパク質品質管理顆粒からストレス顆粒への液固相転移メカニズムの理解, 第47回日本分子生物学会年会, 2024年11月.
7.	松﨑元紀, 齋尾智英 : 電気泳動法によるヘテロなタンパク質分子集合および立体配座変化の評価, 第97回日本生化学会大会, 2024年11月.
8.	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.
9.	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.
10.	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.
11.	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.
12.	松﨑元紀, 奥村正樹 : 多量体分析で解き明かす小胞体ストレスセンサーが細胞応答を量的に調節する仕組み, 第46回日本分子生物学会年会, 2023年12月.
13.	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.
14.	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.
15.	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.
16.	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.
17.	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, -, -, -, Jul. 2023.
18.	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.
19.	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.
20.	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.
21.	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.
22.	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.
23.	松﨑元紀, 金村進吾, 田尻道子, 明石知子, 稲葉謙次, 奥村正樹 : ミスフォールドタンパク質およびジスルフィド結合依存的なIRE1の会合状態制御, 日本農芸化学会2021年度大会, 2021年3月.
24.	Motonori Matsusaki, Shingo Kanemura, Kenji Inaba and Masaki Okumura : Novel Insight into PDI Family-regulated IRE1 Activation/Inactivation, 第20回日本蛋白質科学会年会, Jul. 2020.

その他・研究会:

1.	松﨑元紀, 横山武司, 次田篤史, 金村進吾, 田尻道子, 明石知子, 稲葉謙次, 奥村正樹 : 分子間ジスルフィド結合による小胞体ストレスセンサーIRE1の会合状態制御, 第6回東北大学若手研究者アンサンブルワークショップ, 2021年2月.

特許:

1.	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.
2.	村岡貴博, 岡田隼輔, 奥村正樹, 稲葉謙次, 松﨑元紀 : タンパク質のリフォールディング剤，タンパク質のリフォールディング方法及びタンパク質の再生方法, 特願2018-109769 (2018年6月), 特開2019-210258 (2019年12月), 特許第180022JP01号.

科学研究費補助金 (KAKEN Grants Database @ NII.ac.jp)

分泌経路におけるメゾスケール構造体プロファイリングの開拓 (研究課題/領域番号: 23KK0105 )
細胞内ストレス応答の情報熱力学的な理解 (研究課題/領域番号: 22H04847 )
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 )
IRE1による多次元小胞体ストレス感知メカニズムの解明 (研究課題/領域番号: 22K15278 )
小胞体ストレスセンサーIRE1の活性型ジスルフィドオリゴマー形成機構解明 (研究課題/領域番号: 20K15969 )
小胞体ストレス応答の制御を司るＰＤＩファミリーの分子構造基盤 (研究課題/領域番号: 19J00893 )
研究者番号（90817040）による検索

助教 : 松﨑元紀

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科学研究費補助金 (KAKEN Grants Database @ NII.ac.jp)

助教 : 松﨑 元紀

研究活動

個人のホームページ

専門分野

研究テーマ

著書・論文

学術論文(審査論文):

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国際会議:

国内講演発表:

その他・研究会:

特許:

科学研究費補助金 (KAKEN Grants Database @ NII.ac.jp)

助教 : 松﨑元紀